| 1. |
|
|
| 2. |
|
|
| 3. |
- Falahzadeh, A., et al.
(författare)
-
A New Coastal Crawler Prototype to Expand the Ecological Monitoring Radius of OBSEA Cabled Observatory
- 2023
-
Ingår i: Journal of Marine Science and Engineering. ; 11:4
-
Tidskriftsartikel (refereegranskat)abstract
- The use of marine cabled video observatories with multiparametric environmental data collection capability is becoming relevant for ecological monitoring strategies. Their ecosystem surveying can be enforced in real time, remotely, and continuously, over consecutive days, seasons, and even years. Unfortunately, as most observatories perform such monitoring with fixed cameras, the ecological value of their data is limited to a narrow field of view, possibly not representative of the local habitat heterogeneity. Docked mobile robotic platforms could be used to extend data collection to larger, and hence more ecologically representative areas. Among the various state-of-the-art underwater robotic platforms available, benthic crawlers are excellent candidates to perform ecological monitoring tasks in combination with cabled observatories. Although they are normally used in the deep sea, their high positioning stability, low acoustic signature, and low energetic consumption, especially during stationary phases, make them suitable for coastal operations. In this paper, we present the integration of a benthic crawler into a coastal cabled observatory (OBSEA) to extend its monitoring radius and collect more ecologically representative data. The extension of the monitoring radius was obtained by remotely operating the crawler to enforce back-and-forth drives along specific transects while recording videos with the onboard cameras. The ecological relevance of the monitoring-radius extension was demonstrated by performing a visual census of the species observed with the crawler's cameras in comparison to the observatory's fixed cameras, revealing non-negligible differences. Additionally, the videos recorded from the crawler's cameras during the transects were used to demonstrate an automated photo-mosaic of the seabed for the first time on this class of vehicles. In the present work, the crawler travelled in an area of 40 m away from the OBSEA, producing an extension of the monitoring field of view (FOV), and covering an area approximately 230 times larger than OBSEA's camera. The analysis of the videos obtained from the crawler's and the observatory's cameras revealed differences in the species observed. Future implementation scenarios are also discussed in relation to mission autonomy to perform imaging across spatial heterogeneity gradients around the OBSEA.
|
|
| 4. |
- Keller, Annika, et al.
(författare)
-
Mutations in the gene encoding PDGF-B cause brain calcifications in humans and mice
- 2013
-
Ingår i: Nature Genetics. - : Springer Science and Business Media LLC. - 1061-4036 .- 1546-1718. ; 45:9, s. 1077-
-
Tidskriftsartikel (refereegranskat)abstract
- Calcifications in the basal ganglia are a common incidental finding and are sometimes inherited as an autosomal dominant trait ( idiopathic basal ganglia calcification (IBGC)). Recently, mutations in the PDGFRB gene coding for the platelet-derived growth factor receptor beta (PDGF-R beta) were linked to IBGC. Here we identify six families of different ancestry with nonsense and missense mutations in the gene encoding PDGF-B, the main ligand for PDGF-R beta. We also show that mice carrying hypomorphic Pdgfb alleles develop brain calcifications that show age-related expansion. The occurrence of these calcium depositions depends on the loss of endothelial PDGF-B and correlates with the degree of pericyte and blood-brain barrier deficiency. Thus, our data present a clear link between Pdgfb mutations and brain calcifications in mice, as well as between PDGFB mutations and IBGC in humans.
|
|
| 5. |
|
|
| 6. |
|
|
| 7. |
|
|
| 8. |
|
|
| 9. |
- Falsig, Jeppe, et al.
(författare)
-
Chemical and biophysical insights into the propagation of prion strains
- 2008
-
Ingår i: HFSP JOURNAL. - : Informa UK Limited. - 1955-2068. ; 2:6, s. 332-341
-
Tidskriftsartikel (refereegranskat)abstract
- Transmissible spongiform encephalopathies (TSEs) are lethal infectious neurodegenerative diseases. TSEs are caused by prions, infectious agents lacking informational nucleic acids, and possibly identical with higher-order aggregates of the cellular glycolipoprotein PrPC. Prion strains are derived from TSE isolates that, even after inoculation into genetically identical hosts, cause disease with distinct patterns of protein aggregate deposition, incubation times, morphology of the characteristic brain damage, and cellular tropism. Most of these traits are relatively stable across serial passages. Here we review current techniques for studying prion strain differences in vivo and in cells, and discuss the strain phenomena in the general context of the knowledge gained from modeling prion fibril growth in vitro and in simple organisms.
|
|
| 10. |
- Hornemann, S, et al.
(författare)
-
Mechanistic and structural aspects of the interaction of luminescent conjugated polymers with amyloid oligomers
- 2010
-
Ingår i: Amyloid. - : Informa Healthcare. - 1350-6129 .- 1744-2818. ; 17:S1, s. 98-99
-
Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- Protein misfolding and aggregation diseases, such as e.g. Alzheimer’s disease, are associated by the accumulation of a disease-related protein. The pathogenic mechanisms involved in these confor- mational diseases are only poorly understood. Luminescent-conjugated polymers (LCPs) have been shown as a sensitive tool for detection of amyloid deposits. In contrast to commonly used amyloidotropic dyes such as thioflavins or Congo Red, LCPs are composed of flexible polythiophene chains which allow rotation of the molecule. Upon binding to amyloids, the LCPs alter their spectral properties in a conformation dependent manner. However, there is still limited information available on the binding mechanism and binding properties of the LCPs to amyloid fibrils and oligomers.We have produced recombinant human Aβ1-42 (recAβ1-42) protein in Escherichia coli and purified it by conventional chromatographic techniques in large quantities. The recAβ-protein was incubated in the presence of SDS to induce formation of homogenous, globular Aβ-oligomers with a size of approximately 60 kDa, known as Aβ-globulomers. We present first biophysical and spectroscopic data used to study the binding and structural properties of the complex formed by the globulomers and LCPs with various charged side chains. These data will provide a more detailed knowledge of the binding mode of amyloidogenic probes which is essential for understanding the structural char- acteristics of amyloid fibrils detected by thesemolecules.
|
|
