9,373 research outputs found

    Six Years of ScoX-1 Monitoring with BeppoSAX Wide Field Cameras

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    We performed a systematic analysis of 54 Wide Field Camera (WFC) observations of ScoX-1 available in the BeppoSAX public archive. Observations span over the six years of BeppoSAX mission lifetime and include 690 hr of data. We searched for shifts and shape changes of the Z pattern in the color-color diagrams. We find that the Z pattern occupies most of the time the same locus in the color-color diagram. There are however a few exceptions, which are discussed in detail.Comment: 4 Pages, 4 figures. To appear in Proc. of the BeppoSAX Symposium: "The Restless High-Energy Universe", E.P.J. van den Heuvel, J.J.M. in 't Zand, and R.A.M.J. Wijers (Eds

    Gravitational effects on a rigid Casimir cavity

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    Vacuum fluctuations produce a force acting on a rigid Casimir cavity in a weak gravitational field. Such a force is here evaluated and is found to have opposite direction with respect to the gravitational acceleration; the order of magnitude for a multi-layer cavity configuration is analyzed and experimental detection is discussed, bearing in mind the current technological resources.Comment: 7 pages, Latex. Talk given at the Fifth Leipzig Workshop on Quantum Field Theory under the Influence of External Conditions, September 200

    Epsin 1 Undergoes Nucleocytosolic Shuttling and Its Eps15 Interactor Nh2-Terminal Homology (Enth) Domain, Structurally Similar to Armadillo and Heat Repeats, Interacts with the Transcription Factor Promyelocytic Leukemia Zn2+ Finger Protein (Plzf)

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    Epsin (Eps15 interactor) is a cytosolic protein involved in clathrin-mediated endocytosis via its direct interactions with clathrin, the clathrin adaptor AP-2, and Eps15. The NH2-terminal portion of epsin contains a phylogenetically conserved module of unknown function, known as the ENTH domain (epsin NH2-terminal homology domain). We have now solved the crystal structure of rat epsin 1 ENTH domain to 1.8 Å resolution. This domain is structurally similar to armadillo and Heat repeats of β-catenin and karyopherin-β, respectively. We have also identified and characterized the interaction of epsin 1, via the ENTH domain, with the transcription factor promyelocytic leukemia Zn2+ finger protein (PLZF). Leptomycin B, an antifungal antibiotic, which inhibits the Crm1- dependent nuclear export pathway, induces an accumulation of epsin 1 in the nucleus. These findings suggest that epsin 1 may function in a signaling pathway connecting the endocytic machinery to the regulation of nuclear function

    Automatic synchronisation of the cell cycle in budding yeast through closed-loop feedback control

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    The cell cycle is the process by which eukaryotic cells replicate. Yeast cells cycle asynchronously with each cell in the population budding at a different time. Although there are several experimental approaches to synchronise cells, these usually work only in the short-term. Here, we build a cyber-genetic system to achieve long-term synchronisation of the cell population, by interfacing genetically modified yeast cells with a computer by means of microfluidics to dynamically change medium, and a microscope to estimate cell cycle phases of individual cells. The computer implements a controller algorithm to decide when, and for how long, to change the growth medium to synchronise the cell-cycle across the population. Our work builds upon solid theoretical foundations provided by Control Engineering. In addition to providing an avenue for yeast cell cycle synchronisation, our work shows that control engineering can be used to automatically steer complex biological processes towards desired behaviours similarly to what is currently done with robots and autonomous vehicles

    Insights into the role of reactive sulfhydryl groups of Carbonic Anhydrase III and VII during oxidative damage

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    Carbonic anhydrases (CAs) III and VII are two cytosolic isoforms of the α-CA family which catalyze the physiological reaction of carbon dioxide hydration to bicarbonate and proton. Despite these two enzymes share a 49% sequence identity and present a very similar three-dimensional structure, they show profound differences when comparing the specific activity for CO2 hydration reaction, with CA VII being much more active than CA III. Recently, CA III and CA VII have been proposed to play a new role as scavenger enzymes in cells where oxidative damage occurs. Here, we will examine functional and structural features of these two isoforms giving insights into their newly proposed protective role against oxidative stress
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