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- Borgehammar, Stephan, et al.
(författare)
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The Last Judgement in Medieval Latin Model Sermons
- 2013
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Ingår i: The Last Judgement in Medieval Preaching. - 9782503539676 - 9782503515243 ; , s. 1-17
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Bokkapitel (refereegranskat)abstract
- The article examines specimens from five Latin sermon collections that were widely used as models for sermon composition in the later Middle Ages. Four of the collections were studied in incunable editions. One of the results is that the only day of the eclesiastical year on which one finds a more or less regular discussion of the Last Judgement is the first or second Sunday of Advent. The subject is rarely treated on other Sundays - and where this does occur, the collections suggest the Advent sermons as possible substitutes. Several traditions of depicting the Last Judgement seem to have arisen, one explaining it in analogy with the stages and procedures of a criminal court, which would be known to the audience; another by concentrating on the protagonists in court and identifying the individual listener with one of them. A third tradition involves a frightening description of the signs and perlis of Judgement Day, and yet another lists the many different punishments and explains to the listeners which of their own sins entail which punishment. Instilling fear in the audience seems, however, to be only one of several options: instead, one could concentrate on the fact that the Last Judgement is something that devout Christians should anticipate gladly, as for them it means ultimate justice and eternal salvation. The study gives an idea of the range of ways of treating the Last Judgement and shows that the rhetorical techniques employed are sophisticated, and that the use of images from, and analogies with, daily life is firmly rooted in the Latin tradition. In an Appendix the contents and organization of a pre-1478 edition of Johann Herolt, Sermones Discipuli, are displayed in order to demonstrate the usefulness to scholarship of such indices in early printed sermon collections.
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| 2. |
- Gustavsson, Tobias, et al.
(författare)
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A cytochrome c- fusion protein domain for convenient detection, quantification and enhanced production of membrane proteins in Escherichia coli - expression and characterization of cytochrome-tagged complex I subunits
- 2010
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Ingår i: Protein Science. - : Wiley. - 1469-896X .- 0961-8368. ; 19:8, s. 1445-1460
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Tidskriftsartikel (refereegranskat)abstract
- Overproduction of membrane proteins can be a cumbersome task, particularly if high yields are desirable. NADH:quinone oxidoreductase (complex I) contains several very large membrane-spanning protein subunits that hitherto have been impossible to express individually in any appreciable amounts in Escherichia coli. The polypeptides contain no prosthetic groups and are poorly antigenic, making optimization of protein production a challenging task. In this work the C-terminal ends of the complex I subunits NuoH, NuoL, NuoM and NuoN from E. coli complex I and the bona fide antiporters MrpA and MrpD were genetically fused to the cytochrome c domain of Bacillus subtilis cytochrome c(550). Compared to other available fusion-protein tagging systems, the cytochrome c has several advantages. The heme is covalently bound, renders the proteins visible by optical spectroscopy, and can be used to monitor, quantify and determine the orientation of the polypeptides in a plethora of experiments. For the antiporter-like subunits NuoL, NuoM and NuoN and the real antiporters MrpA and MrpD, unprecedented amounts of holo-cytochrome fusion proteins could be obtained in E. coli. The NuoHcyt polypeptide was also efficiently produced, but heme insertion was less effective in this construct. The cytochrome c(550) domain in all the fusion proteins exhibited normal spectra and redox properties, with an E(m) of about +170 mV. The MrpA and MrpD antiporters remained functional after being fused to the cytochrome c-tag. Finally, a his-tag could be added to the cytochrome domain, without any perturbations to the cytochrome properties, allowing efficient purification of the overexpressed fusion proteins.
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| 3. |
- Johnson, Toby, et al.
(författare)
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Blood Pressure Loci Identified with a Gene-Centric Array.
- 2011
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Ingår i: American Journal of Human Genetics. - : Elsevier BV. - 1537-6605 .- 0002-9297. ; 89:6, s. 688-700
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Tidskriftsartikel (refereegranskat)abstract
- Raised blood pressure (BP) is a major risk factor for cardiovascular disease. Previous studies have identified 47 distinct genetic variants robustly associated with BP, but collectively these explain only a few percent of the heritability for BP phenotypes. To find additional BP loci, we used a bespoke gene-centric array to genotype an independent discovery sample of 25,118 individuals that combined hypertensive case-control and general population samples. We followed up four SNPs associated with BP at our p < 8.56× 10(-7) study-specific significance threshold and six suggestively associated SNPs in a further 59,349 individuals. We identified and replicated a SNP at LSP1/TNNT3, a SNP at MTHFR-NPPB independent (r(2) = 0.33) of previous reports, and replicated SNPs at AGT and ATP2B1 reported previously. An analysis of combined discovery and follow-up data identified SNPs significantly associated with BP at p < 8.56× 10(-7) at four further loci (NPR3, HFE, NOS3, and SOX6). The high number of discoveries made with modest genotyping effort can be attributed to using a large-scale yet targeted genotyping array and to the development of a weighting scheme that maximized power when meta-analyzing results from samples ascertained with extreme phenotypes, in combination with results from nonascertained or population samples. Chromatin immunoprecipitation and transcript expression data highlight potential gene regulatory mechanisms at the MTHFR and NOS3 loci. These results provide candidates for further study to help dissect mechanisms affecting BP and highlight the utility of studying SNPs and samples that are independent of those studied previously even when the sample size is smaller than that in previous studies.
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