Bandwidth Allocation for a Revenue-Aware Network Utility Maximisation

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Evaluando los niveles tróficos de dos tiburones oceánicos del Océano Pacífico suroriental

Indexación: Web of ScienceStable isotope analyses for shortfin mako (Isurus oxyrinchus) and blue sharks (Prionace glauca) were conducted to assess their trophic position in two periods of time (before 1980 and after 2000) in the Southeastern Pacific waters (SEP). Both sharks showed that their trophic position decreased over time (P < 0.05). Many factors could be involved in this change such as dietary shifts, prey availability, or indirect fishing effects in SEP waters.RESUMEN. Para evaluar los niveles tróficos de los tiburones marrajo (Isurus oxyrinchus) y azulejo (Prionace glauca) en dos períodos de tiempo (previo a 1980 y posterior al 2000) en aguas del Pacífico suroriental (SEP), se realizaron análisis de isótopos estables. Ambos tiburones mostraron un descenso del nivel trófico en el tiempo (P < 0,05). Varios son los factores que pueden estar involucrados en este evento, como los cambios dietarios, la disponibilidad de las presas o los efectos indirectos de la pesquería en aguas del Pacífico suroriental.http://www.lajar.cl/pdf/imar/v44n2/Art%C3%ADculo_44_2_25.pd

Reinforcement learning for resource allocation in LEO satellite networks

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Do consumers pay voluntarily? The case of online music

The paper analyses the payment behaviour of customers of the online music label Magnatune. Customers may pay what they want for albums, as long as the payment is within a given price range ($5-$18). Magnatune's comprehensive pre-purchase access facilitates music discovery and allows an informed buying decision setting it apart from conventional online music stores

Prion Diseases: A Unique Transmissible Agent or a Model for Neurodegenerative Diseases?

The accumulation and propagation in the brain of misfolded proteins is a pathological hallmark shared by many neurodegenerative diseases such as Alzheimer’s disease (Aβ and tau), Parkinson’s disease (α-synuclein), and prion disease (prion protein). Currently, there is no epidemiological evidence to suggest that neurodegenerative disorders are infectious, apart from prion diseases. However, there is an increasing body of evidence from experimental models to suggest that other pathogenic proteins such as Aβ and tau can propagate in vivo and in vitro in a prion-like mechanism, inducing the formation of misfolded protein aggregates such as amyloid plaques and neurofibrillary tangles. Such similarities have raised concerns that misfolded proteins, other than the prion protein, could potentially transmit from person-to-person as rare events after lengthy incubation periods. Such concerns have been heightened following a number of recent reports of the possible inadvertent transmission of Aβ pathology via medical and surgical procedures. This review will provide a historical perspective on the unique transmissible nature of prion diseases, examining their impact on public health and the ongoing concerns raised by this rare group of disorders. Additionally, this review will provide an insight into current evidence supporting the potential transmissibility of other pathogenic proteins associated with more common neurodegenerative disorders and the potential implications for public health

Understanding Intra-Species and Inter-Species Prion Conversion and Zoonotic Potential Using Protein Misfolding Cyclic Amplification

Prion diseases are fatal neurodegenerative disorders that affect humans and animals, and can also be transmitted from animals to humans. A fundamental event in prion disease pathogenesis is the conversion of normal host prion protein (PrPC) to a disease-associated misfolded form (PrPSc). Whether or not an animal prion disease can infect humans cannot be determined a priori. There is a consensus that classical bovine spongiform encephalopathy (C-type BSE) in cattle transmits to humans, and that classical sheep scrapie is of little or no risk to human health. However, the zoonotic potential of more recently identified animal prion diseases, such as atypical scrapie, H-type and L-type BSE and chronic wasting disease (CWD) in cervids, remains an open question. Important components of the zoonotic barrier are (i) physiological differences between humans and the animal in question, (ii) amino acid sequence differences of the animal and human PrPC, and (iii) the animal prion strain, enciphered in the conformation of PrPSc. Historically, the direct inoculation of experimental animals has provided essential information on the transmissibility and compatibility of prion strains. More recently, cell-free molecular conversion assays have been used to examine the molecular compatibility on prion replication and zoonotic potential. One such assay is Protein Misfolding Cyclic Amplification (PMCA), in which a small amount of infected tissue homogenate, containing PrPSc, is added as a seed to an excess of normal tissue homogenate containing PrPC, and prion conversion is accelerated by cycles of incubation and ultrasonication. PMCA has been used to measure the molecular feasibility of prion transmission in a range of scenarios using genotypically homologous and heterologous combinations of PrPSc seed and PrPC substrate. Furthermore, this method can be used to speculate on the molecular profile of PrPSc that might arise from a zoonotic transmission. We discuss the experimental approaches that have been used to model both the intra- and inter-species molecular compatibility of prions, and the factors affecting PrPc to PrPSc conversion and zoonotic potential. We conclude that cell-free prion protein conversion assays, especially PMCA, are useful, rapid and low-cost approaches for elucidating the mechanisms of prion propagation and assessing the risk of animal prions to humans

Variant CJD: Reflections a Quarter of a Century on

Twenty-five years has now passed since variant Creutzfeldt-Jakob disease (vCJD) was first described in the United Kingdom (UK). Early epidemiological, neuropathological and biochemical investigations suggested that vCJD represented a new zoonotic form of human prion disease resulting from dietary exposure to the bovine spongiform encephalopathy (BSE) agent. This hypothesis has since been confirmed though a large body of experimental evidence, predominantly using animal models of the disease. Today, the clinical, pathological and biochemical phenotype of vCJD is well characterized and demonstrates a unique and remarkably consistent pattern between individual cases when compared to other human prion diseases. While the numbers of vCJD cases remain reassuringly low, with 178 primary vCJD cases reported in the UK and a further 54 reported worldwide, concerns remain over the possible appearance of new vCJD cases in other genetic cohorts and the numbers of asymptomatic individuals in the population harboring vCJD infectivity. This review will provide a historical perspective on vCJD, examining the origins of this acquired prion disease and its association with BSE. We will investigate the epidemiology of the disease along with the unique clinicopathological and biochemical phenotype associated with vCJD cases. Additionally, this review will examine the impact vCJD has had on public health in the UK and the ongoing concerns raised by this rare group of disorders

Susceptibility of Human Prion Protein to Conversion by Chronic Wasting Disease Prions

Chronic wasting disease (CWD) is a contagious and fatal neurodegenerative disease and a serious animal health issue for deer and elk in North America. The identification of the first cases of CWD among free-ranging reindeer and moose in Europe brings back into focus the unresolved issue of whether CWD can be zoonotic like bovine spongiform encephalopathy. We used a cell-free seeded protein misfolding assay to determine whether CWD prions from elk, white-tailed deer, and reindeer in North America can convert the human prion protein to the disease-associated form. We found that prions can convert, but the efficiency of conversion is affected by polymorphic variation in the cervid and human prion protein genes. In view of the similarity of reindeer, elk, and white-tailed deer in North America to reindeer, red deer, and roe deer, respectively, in Europe, a more comprehensive and thorough assessment of the zoonotic potential of CWD might be warranted

First observation and measurement of the resonant structure of the lambda_b->lambda_c pi-pi+pi- decay mode

We present the first observation of the lambda_b->lambda_c pi-pi+pi- decay using data from an integrated luminosity of approximately 2.4 fb-1 of ppbar collisions at ECM=1.96 TeV, collected with the CDF II detector at the Fermilab Tevatron. We also present the first observation of the resonant decays lambda_b->sigma_c(2455)0 pi+pi- ->lambda_c pi-pi+pi-, lambda_b->sigma_c(2455)++ pi-pi- ->lambda_c pi-pi+pi-, lambda_b->lambda_c(2595)+ pi- ->lambda_c pi-pi+pi- and lambda_b->lambda_c(2625)+ pi- ->lambda_c pi-pi+pi-, and measure their relative branching ratios.Comment: 3 pages, 3 figures, to appear in the proceedings of LEPTON PHOTON 2009, Hamburg, German