111 research outputs found

    The European Archive of Historical Earthquake Data (AHEAD): compilation, results, and perspectives.

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    Historical seismic catalogues in Europe have been mostly compiled on a national basis starting from historical data collected and interpreted according to different procedures and varied levels of formalization. With few exceptions, the macroseismic data that stand behind the catalogues are not available, or simply never existed. The present-day knowledge on past seismicity in Europe is consequently far from being homogeneous. This situation affected the past efforts for the compilation of homogeneous, continent-wide catalogues and still restrains the ongoing initiatives on this topic. To overcome this situation, the NERIES NA4 project realized the European Archive of Historical Earthquake Data (AHEAD). AHEAD collects and puts together in a critical way the background information supporting European earthquakes between the years 1000 and 1963. The collected information consists of the most significant, or recent, material supporting an earthquake, such as: i) studies that interpret the historical records in terms of Macroseismic Data-Points (MDPs); ii) studies that provide the historical records but not interpreted in terms of MDPs; iii) parameters from catalogues, only. AHEAD contains entries related to more than 10.000 earthquakes, and the inventoried material is made available through the web. It also provides in a standardized database the MDPs that support about the 60% of the listed earthquakes. For a large number of them such MDPs have been released for the first time by partner institutions in the framework of NERIES NA4. AHEAD is conceived as an interactive tool for representing and improving the knowledge on historical earthquakes, with the aim of making it homogeneous at a European level. Through the archive researchers can easily: 1) trace back the information supporting each earthquake in order to reappraise and improve the knowledge of it; 2) compare the different studies on each earthquake and select a preferred one. This is, for example, the procedure followed for the selection of data upon which the NERIES NA4 European Earthquake Catalogue has been compiled. 3) help keeping the archive as much up-to-date as possible, commenting studies, data, and parameters and feeding it with fresh studies

    Archive of Historical Earthquake Data for the European-Mediterranean Area

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    The importance of historical earthquake data is largely recognized by both seismologists and engineers, who use such data in a wide range of applications

    Low M r Phosphotyrosine Protein Phosphatase Associates and Dephosphorylates p125 Focal Adhesion Kinase, Interfering with Cell Motility and Spreading

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    Low M(r) phosphotyrosine protein phosphatase interferes in vivo with the activation of several growth factor receptors and is transiently redistributed, following cell stimulation with platelet-derived growth factor, from the cytosol to the cytoskeleton. We demonstrate here that this phosphatase also participates in the regulation of cell spreading and migration, pointing to its involvement in cytoskeleton organization. Low M(r) phosphotyrosine protein phosphatase-overexpressing fibroblasts are, indeed, less spread than controls and display a significantly decreased number of focal adhesions and increased cell motility. Furthermore, p125 focal adhesion kinase is associated to, and dephosphorylated by, low M(r) phosphotyrosine protein phosphatase both in vitro and in vivo. This event is consistent with an altered association of pp60(src) with focal adhesion kinase. The activation of extracellular signal-regulated kinase, another well known event downstream of the focal adhesion kinase, is also affected. On the other hand, cells overexpressing the dominant-negative form of low M(r) phosphotyrosine protein phosphatase exhibit hyperphosphorylated focal adhesion kinase, reduced motility, and an increased number of focal adhesions, which are distributed all over the ventral cell surface. Taken together, the results reported here are in keeping with low M(r) phosphotyrosine protein phosphatase participation in FAK-mediated focal adhesion remodeling

    The IT framework of the European Archive of Historical Earthquake Data (AHEAD)

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    The European Archive of Historical EArthquake Data (AHEAD) has been developed in the frame of the EC project NERIES and maintained in the frame of the EC project SHARE.AHEAD makes available on the web the result of a networked historical earthquake data research, formalised in terms of studies (papers, reports, macroseismic data points, etc). It provides an updated wealth of data that are unique for many European events in the time-window 1000-1963.A series of IT solutions have been developed in order to support both the research and the networking activities carried out within the building process of AHEAD. The resulting framework is an equally balanced effort in both the back-end and front-end design and implementation, a key feature in a research approach very much human-centred, where the quantity of data is small if compared to terabytes of instrumental data.AHEAD is composed of five mutually dependent data-components: 1) the “Digital Library”, where all the historical earthquake studies are stored and described by bibliographical metadata, 2) the “Consensus Earthquake Inventory”, where the relevant macroseismic data (event date, epicentral area, number of macroseismic data-point, maximum observed intensity) are extrapolated, the best available information are selected and fake earthquakes are highlighted, 3) the “European Macroseismic Database”, where all the available macroseismic data-points (MDPs) are stored, 4) the “Parameters Laboratory”, where earthquakes parameterisation methods are applied to MDPs in order to obtain epicentral locations and magnitudes and 5) the “European Earthquake Catalogue”.The presentation will demonstrate the adopted IT solutions separately for the back-end and the front-end, both for the access-restricted website and the general-purpose implementation designed to be included in the “Earthquake Data Portal”, developed within the EC project NERIES, which targets a much broader scientific community

    Low Mr phosphotyrosine protein phosphatase activity on fibroblast growth factor receptor is not associated with enzyme translocation

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    AbstractFibroblast growth factor receptor (class IV) shares a certain degree of similarity with class III members like platelet-derived growth factor and macrophage-colony-stimulating factor receptors, which, once activated, are substrates of low Mr phosphotyrosine protein phosphatase. Up until now no phosphotyrosine phosphatase has been shown to act on this receptor in vivo. Here we demonstrate that low Mr phosphotyrosine protein phosphatase is able to reduce receptor tyrosine phosphorylation and cell proliferation in response to basic fibroblast growth factor. Contrary to what was previously observed for platelet-derived growth factor, during cell stimulation with basic fibroblast growth factor, no enzyme redistribution among cellular compartments is observed

    The Colony-Stimulating Factor-1 (CSF-1) Receptor Sustains ERK1/2 Activation and Proliferation in Breast Cancer Cell Lines

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    Breast cancer is the second leading cause of cancer-related deaths in western countries. Colony-Stimulating Factor-1 (CSF-1) and its receptor (CSF-1R) regulate macrophage and osteoclast production, trophoblast implantation and mammary gland development. The expression of CSF-1R and/or CSF-1 strongly correlates with poor prognosis in several human epithelial tumors, including breast carcinomas. We demonstrate that CSF-1 and CSF-1R are expressed, although at different levels, in 16/17 breast cancer cell lines tested with no differences among molecular subtypes. The role of CSF-1/CSF-1R in the proliferation of breast cancer cells was then studied in MDAMB468 and SKBR3 cells belonging to different subtypes. CSF-1 administration induced ERK1/2 phosphorylation and enhanced cell proliferation in both cell lines. Furthermore, the inhibition of CSF-1/CSF-1R signaling, by CSF-1R siRNA or imatinib treatment, impaired CSF-1 induced ERK1/2 activation and cell proliferation. We also demonstrate that c-Jun, cyclin D1 and c-Myc, known for their involvement in cell proliferation, are downstream CSF-1R in breast cancer cells. The presence of a proliferative CSF-1/CSF-1R autocrine loop involving ERK1/2 was also found. The wide expression of the CSF-1/CSF-1R pair across breast cancer cell subtypes supports CSF-1/CSF-1R targeting in breast cancer therapy

    ProCMD: a database and 3D web resource for protein C mutants

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    Background: Activated Protein C (ProC) is an anticoagulant plasma serine protease which also plays an important role in controlling inflammation and cell proliferation. Several mutations of the gene are associated with phenotypic functional deficiency of protein C, and with the risk of developing venous thrombosis. Structure prediction and computational analysis of the mutants have proven to be a valuable aid in understanding the molecular aspects of clinical thrombophilia. Results: We have built a specialized relational database and a search tool for natural mutants of protein C. It contains 195 entries that include 182 missense and 13 stop mutations. A menu driven search engine allows the user to retrieve stored information for each variant, that include genetic as well as structural data and a multiple alignment highlighting the substituted position. Molecular models of variants can be visualized with interactive tools; PDB coordinates of the models are also available for further analysis. Furthermore, an automatic modelling interface allows the user to generate multiple alignments and 3D models of new variants. Conclusion: ProCMD is an up-to-date interactive mutant database that integrates phenotypical descriptions with functional and structural data obtained by computational approaches. It will be useful in the research and clinical fields to help elucidate the chain of events leading from a molecular defect to the related disease. It is available for academics at the URL http://www.itb.cnr.it/procmd/
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