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- de Jong, R. S., et al.
(författare)
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4MOST : Project overview and information for the First Call for Proposals
- 2019
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Ingår i: The Messenger. - : European Southern Observatory. - 0722-6691. ; 175, s. 3-11
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- We introduce the 4-metre Multi-Object Spectroscopic Telescope (4MOST), a new high-multiplex, wide-field spectroscopic survey facility under development for the four-metre-class Visible and Infrared Survey Telescope for Astronomy (VISTA) at Paranal. Its key specifications are: a large field of view (FoV) of 4.2 square degrees and a high multiplex capability, with 1624 fibres feeding two low-resolution spectrographs (R = λ/Δλ ~ 6500), and 812 fibres transferring light to the high-resolution spectrograph (R ~ 20 000). After a description of the instrument and its expected performance, a short overview is given of its operational scheme and planned 4MOST Consortium science; these aspects are covered in more detail in other articles in this edition of The Messenger. Finally, the processes, schedules, and policies concerning the selection of ESO Community Surveys are presented, commencing with a singular opportunity to submit Letters of Intent for Public Surveys during the first five years of 4MOST operations.
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- Bolognesi, B, et al.
(författare)
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The N-terminus of amyloid-beta plays a crucial role in its aggregation and toxicity
- 2010
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Ingår i: The FEBS Journal. - : Wiley-Blackwell. - 1742-464X .- 1742-4658. ; 277:Suppl. 1, s. 79-80
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- The aggregation of Amyloid Beta (Aß) peptide into insolubleamyloid fibrils that deposit in the brain is one of the primarypathogenic events in Alzheimer’s disease. We have previouslyshown, using a Drosophila model of Aß toxicity, that the N terminus of the Aß peptide, despite being unstructured in themature Aß fibril, nonetheless affects Aß induced neurodegeneration in vivo. In order to understand the contribution of the N terminusof Aß to its aggregation behaviour, we have investigated anumber of rationally designed N-terminal mutants in vitro. We find that single amino acid mutations in this region affect significantlythe kinetics of Aß aggregation in vitro as measured by arange of spectroscopic techniques. Furthermore, we observe striking differences in the morphology of the aggregated speciesformed by these different Aß mutants when imaged with TEM or AFM and also in the ß-sheet content of their mature fibrils. Interestingly, mutants with an increased net charge or lower hydrophobicity tend to show slower aggregation kinetics, and to form more ordered aggregates whereas mutations that reduce net charge or increase hydrophobicity favour faster aggregation kinetics and poorly structured aggregates. In addition, the exposed hydrophobicity of aggregates formed in the early stages of aggregation is correlated to their toxicity. These findings demonstrate not only that the N-terminus of the Aß peptide plays a crucial role in its aggregation and toxicity but also suggest that this region of Aß may modulate in vivo toxicity by altering the conformations of aggregates that it forms.
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- Settele, Josef, et al.
(författare)
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Rice ecosystem services in South-east Asia
- 2018
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Ingår i: Paddy and Water Environment. - : Springer. - 1611-2490 .- 1611-2504. ; 16:2, s. 211-224
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)
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