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| 2. |
- Bjurling, Oscar, et al.
(författare)
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Enabling Human-Autonomy Teaming in Aviation : A Framework to Address Human Factors in Digital Assistants Design
- 2024
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Ingår i: Journal of Physics, Conference Series. - : Institute of Physics. - 1742-6588 .- 1742-6596. ; 2716
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Tidskriftsartikel (refereegranskat)abstract
- The introduction of artificial intelligence (AI) tools in aviation necessitates more research into human-autonomy teaming in these domain settings. This paper describes the development of a design framework for supporting Human Factors novices in considering human factors, improving human-autonomy collaboration, and maintaining safety when developing AI tools for aviation settings. Combining elements of Hierarchical Task Analysis, Coactive Design, and Types and Levels of Autonomy, the design framework provides guidance in three phases: modelling and understanding the existing system and associated tasks; producing a new function allocation for optimal Human-Autonomy Teaming (HAT); and assessing HAT-related risks of the proposed design. In this framework, designers generate a comprehensive set of design considerations to support subsequent development processes. Framework limitations and future research avenues are discussed.
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| 3. |
- Michel, M., et al.
(författare)
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Small-molecule activation of OGG1 increases oxidative DNA damage repair by gaining a new function
- 2022
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Ingår i: Science. - Stockholm : American Association for the Advancement of Science. - 0036-8075 .- 1095-9203. ; 376:6600, s. 1471-1476
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Tidskriftsartikel (refereegranskat)abstract
- Oxidative DNA damage is recognized by 8-oxoguanine (8-oxoG) DNA glycosylase 1 (OGG1), which excises 8-oxoG, leaving a substrate for apurinic endonuclease 1 (APE1) and initiating repair. Here, we describe a small molecule (TH10785) that interacts with the phenylalanine-319 and glycine-42 amino acids of OGG1, increases the enzyme activity 10-fold, and generates a previously undescribed b,d-lyase enzymatic function. TH10785 controls the catalytic activity mediated by a nitrogen base within its molecular structure. In cells, TH10785 increases OGG1 recruitment to and repair of oxidative DNA damage. This alters the repair process, which no longer requires APE1 but instead is dependent on polynucleotide kinase phosphatase (PNKP1) activity. The increased repair of oxidative DNA lesions with a small molecule may have therapeutic applications in various diseases and aging. © 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works
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| 4. |
- Muller, D, et al.
(författare)
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Competitive adsorption of gelatin and sodium dodecylbenzenesulfonate at hydrophobic surfaces
- 1998
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Ingår i: Langmuir. - 0743-7463 .- 1520-5827. ; 14, s. 3107-3114
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Tidskriftsartikel (refereegranskat)abstract
- The competitive adsorption of gelatin and sodium dodecylbenzenesulfonate (SDBS) at hydrophobic surfaces was investigated with surface and interfacial tension measurements, ellipsometry, surface plasmon resonance spectroscopy (SPR), and total internal reflectance fluorescence spectroscopy (TIRF). From both ellipsometry and SPR, initial additions of SDBS after gelatin preadsorption were found to result in a total adsorbed amount increase, as well as in a swelling of the adsorbed layer. At higher SDBS concentrations, both the total adsorbed amount and the amount of gelatin adsorbed decrease, which was observed from ellipsometry, SPR, and TIRF. From surface and interfacial tension measurements, it was found that the critical aggregation concentration (cac) for the SDBS-gelatin system decreases with decreasing pH. Analogous to this, ellipsometry, SPR, and TIRF indicate that the SDBS concentration required to cause a significant decrease in the gelatin adsorbed amount decreases with decreasing pH. The desorption therefore seems to be correlated to the SDBS binding to the adsorbed gelatin molecules rather than to purely competitive adsorption.
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| 5. |
- Muller, D, et al.
(författare)
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Interaction of gelatin and sodium dodecyl benzene sulphonate at oil and water interfaces
- 1997
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Ingår i: Imaging Science Journal. - 1368-2199 .- 1743-131X. ; 45, s. 229-235
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Tidskriftsartikel (refereegranskat)abstract
- Interaction between sodium dodecyl benzene sulphonate (SDBS) and gelatin was studied in relation to emulsification behaviour and emulsion stability. We chose two different oils to study influences of oil phase characteristics, namely, tricresyl phosphate (TCP) as an oil with polar and slightly hydrophilic nature, and n-docedane (nC12) as its apolar contrast. Our interfacial tension measurements showed that both TCP and n-C12 give critical values (i.e., cac and cmc) very close to those of surface tension measurement. This result indicates that the complexation behaviour in bulk solution is independent of the presence or the nature of the oil phase. Absolute tension values above the cmc and slope values at the cmc in gelatin free systems, however, imply SDBC's weaker adsorption to TCP than to n-C12. Our emulsification results for the TCP system revealed the existence of an optiomal point for emulsion stability in the SDBS concentration region between the cac and the cmc. Above this point, emulsion stability deteriorates remarkably. The behaviour is in line with our findings from the dynamic sorption expriments (ellipsometry, TIRF, and SPR) reported elsewhere, which showed a rapid desorption of gelatin from the hydrophobic surfaces above the cac. The results suggest that the adsorption of gelatin/ surfactant complexes at the interface is a key factor for stability of the polar oil emulsion system. Contrary to that , the n-c12 system did not show any deterioration, even above the cmc, which is presumably due to a strong double layer effect from the firmly adsorbed layer of SDBS at the interface.
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