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Sökning: WFRF:(Johansson A. G. M.) > (2010-2014) > RISE

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1.
  • Merlone, Andrea, et al. (författare)
  • A new challenge for meteorological measurements : The meteoMet project-Metrology for meteorology
  • 2013
  • Ingår i: AIP Conference Proceedings. - : AIP. - 0094-243X .- 1551-7616. - 9780735411784 ; , s. 1030-1035
  • Konferensbidrag (refereegranskat)abstract
    • Climate change and its consequences require immediate actions in order to safeguard the environment and economy in Europe and in the rest of world. Aiming to enhance data reliability and reduce uncertainties in climate observations, a joint research project called MeteoMet-Metrology for Meteorology started in October 2011 coordinated by the Italian Istituto Nazionale di Ricerca Metrologica (INRiM). The project is focused on the traceability of measurements involved in climate change: surface and upper air measurements of temperature, pressure, humidity, wind speed and direction, solar irradiance and reciprocal influences between measurands. This project will provide the first definition at the European level of validated climate parameters with associated uncertainty budgets and novel criteria for interpretation of historical data series. The big challenge is the propagation of a metrological measurement perspective to meteorological observations. When such an approach will be adopted the requirement of reliable data and robust datasets over wide scales and long terms could be better met.
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2.
  • Carlred, Louise M, 1985, et al. (författare)
  • Simultaneous imaging of amyloid-β and lipids in brain tissue using antibody-coupled liposomes and time-of-flight secondary ion mass spectrometry
  • 2014
  • Ingår i: Journal of the American Chemical Society. - : American Chemical Society (ACS). - 1520-5126 .- 0002-7863. ; 136:28, s. 9973-9981
  • Tidskriftsartikel (refereegranskat)abstract
    • The spatial localization of amyloid-β peptide deposits, the major component of senile plaques in Alzheimer's disease (AD), was mapped in transgenic AD mouse brains using time-of-flight secondary ion mass spectrometry (ToF-SIMS), simultaneously with several endogenous molecules that cannot be mapped using conventional immunohistochemistry imaging, including phospholipids, cholesterol and sulfatides. Whereas the endogenous lipids were detected directly, the amyloid-β deposits, which cannot be detected as intact entities with ToF-SIMS because of extensive ion-induced fragmentation, were identified by specific binding of deuterated liposomes to antibodies directed against amyloid-β. Comparative investigation of the amyloid-β deposits using conventional immunohistochemistry and fluorescence microscopy suggests similar sensitivity but a more surface-confined identification due to the shallow penetration depth of the ToF-SIMS signal. The recorded ToF-SIMS images thus display the localization of lipids and amyloid-β in a narrow (∼10 nm) two-dimensional plane at the tissue surface. As compared to a frozen nontreated tissue sample, the liposome preparation protocol generally increased the signal intensity of endogenous lipids, likely caused by matrix effects associated with the removal of salts, but no severe effects on the tissue integrity and the spatial distribution of lipids were observed with ToF-SIMS or scanning electron microscopy (SEM). This method may provide an important extension to conventional tissue imaging techniques to investigate the complex interplay of different kinds of molecules in neurodegenerative diseases, in the same specimen. However, limitations in target accessibility of the liposomes as well as unspecific binding need further consideration. © 2014 American Chemical Society.
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