| 1. |
- Campbell, M, et al.
(författare)
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Detection of single electrons by means of a Micromegas-covered Medipix2 pixel CMOS readout circuit
- 2005
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Ingår i: Nuclear Instruments and Methods in Physics Research Section A. - : Elsevier BV. - 0168-9002 .- 1872-9576. ; 540:2-3, s. 295-304
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Tidskriftsartikel (refereegranskat)abstract
- A small drift chamber was read out by means of a MediPix2 readout chip as a direct anode. A Micromegas foil was placed above the chip, and electron multiplication occurred in the gap. With a He/isobutane 80/20 mixture, gas multiplication factors up to tens of thousands were achieved, resulting in an efficiency for detecting single electrons of better than 90%. We recorded many frames containing 2D images with tracks from cosmic muons. Along these tracks, electron clusters were observed, as well as δ-rays.
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| 2. |
- Boekel, Carolina, 1977-
(författare)
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Integration and topology of membrane proteins
- 2009
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Doktorsavhandling (övrigt vetenskapligt/konstnärligt)abstract
- Membrane proteins comprise around 20-30% of most proteomes. They play important roles in most biochemical pathways. All receptors and ion channels are membrane proteins, which make them attractive targets for drug design. Membrane proteins insert and fold co-translationally into the endoplasmic reticular membrane of eukaryotic cells. The protein-conducting channel that inserts the protein into the membrane is called Sec61 translocon, which is a hetero-oligomeric channel that allows transmembrane segments to insert laterally into the lipid bilayer. The focus of this thesis is how the translocon recognizes the transmembrane helices and integrates them into the membrane.We have investigated the sequence requirements for the translocon-mediated integration of a transmembrane α-helix into the ER by challenging the Sec61 translocon with designed polypeptide segments in an in vitro expression system that allows a quantitative assessment of membrane insertion efficiency. Our studies suggest that helices might interact with each other already during the membrane-insertion step, possibly forming helical hairpins that partition into the membrane as a single unit. Further, the insertion efficiency for Nin-Cout vs. Nout-Cin transmembrane helices and the integration efficiency of Alzheimer’s Aβ-peptide fragments has been investigated.Finally, detailed topology mapping was performed on two biologically interesting proteins with unknown topology, the human seipin protein and Drosophila melanogaster odorant receptor OR83b.
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| 6. |
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| 7. |
- Juncker, Agnieszka S, et al.
(författare)
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Sequence-based feature prediction and annotation of proteins
- 2009
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Ingår i: Genome biology. - : Springer Science and Business Media LLC. - 1465-6914 .- 1465-6906. ; 10:2, s. 206-
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Tidskriftsartikel (refereegranskat)abstract
- A recent trend in computational methods for annotation of protein function is that many prediction tools are combined in complex workflows and pipelines to facilitate the analysis of feature combinations, for example, the entire repertoire of kinase-binding motifs in the human proteome.
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| 8. |
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| 9. |
- Lundin, Carolina, et al.
(författare)
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Membrane topology of the Drosophila OR83b odorant receptor
- 2007
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Ingår i: FEBS Letters. - : Wiley. - 0014-5793 .- 1873-3468. ; 581:29, s. 5601-5604
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Tidskriftsartikel (refereegranskat)abstract
- By analogy to mammals, odorant receptors (ORs) in insects, such as Drosophila melanogaster, have long been thought to belong to the G-protein coupled receptor (GPCR) superfamily. However, recent work has cast doubt on this assumption and has tentatively suggested an inverted topology compared to the canonical N(out) - C(in) 7 transmembrane (TM) GPCR topology, at least for some Drosophila ORs. Here, we report a detailed topology mapping of the Drosophila OR83b receptor using engineered glycosylation sites as topology markers. Our results are inconsistent with a classical GPCR topology and show that OR83b has an intracellular N-terminus, an extracellular C-terminus, and 7TM helices.
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