Identity, Ideology, and Malleability
In: Studies in conflict and terrorism, Band 34, Heft 10, S. 820-824
ISSN: 1521-0731
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In: Studies in conflict and terrorism, Band 34, Heft 10, S. 820-824
ISSN: 1521-0731
In: Studies in conflict & terrorism, Band 34, Heft 10, S. 820-825
ISSN: 1057-610X
In: MCU Journal, Band 7, Heft 1, S. 30-45
ISSN: 2164-4217
In: The Evolution of the Global Terrorist Threat
Through a mixed methods research design, we address normative aspects of news recommendation engines by examining whether search personalisation and news diversity are evident on Google News in the UK. Firstly, in a quasi-experimental design, we asked a diverse set of participants (N=78) to search Google News using four search terms and report the first five articles recommended for each term. We found little evidence of news personalisation, which challenges the claim that news search algorithms contribute to weakened viewpoint diversity. We also found a high degree of homogeneity in news search results, with legacy media brands dominating. Secondly, we conducted a manual content analysis of the articles recommended by Google News for our search terms (N=192), focusing on favourability towards each term. We found that while there was little relationship between the favourability slant of the articles and political leanings of participants, there were two exceptions: self-identified right-wing participants were more likely to see unfavourable stories about 1) immigration, and 2) a left-wing politician. This reopens the question of news search engines' contributions to polarisation and viewpoint diversity for certain news consumers.
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In: Studies in conflict and terrorism, Band 34, Heft 11, S. 825-842
ISSN: 1521-0731
In: Studies in conflict & terrorism, Band 34, Heft 11, S. 825-842
ISSN: 1057-610X
World Affairs Online
The increased interest in using monoclonal antibodies (mAbs) as a platform for biopharmaceuticals has led to the need for new analytical techniques that can precisely assess physicochemical properties of these large and very complex drugs for the purpose of correctly identifying quality attributes (QA). One QA, higher order structure (HOS), is unique to biopharmaceuticals and essential for establishing consistency in biopharmaceutical manufacturing, detecting process-related variations from manufacturing changes and establishing comparability between biologic products. To address this measurement challenge, two-dimensional nuclear magnetic resonance spectroscopy (2D-NMR) methods were introduced that allow for the precise atomic-level comparison of the HOS between two proteins, including mAbs. Here, an inter-laboratory comparison involving 26 industrial, government and academic laboratories worldwide was performed as a benchmark using the NISTmAb, from the National Institute of Standards and Technology (NIST), to facilitate the translation of the 2D-NMR method into routine use for biopharmaceutical product development. Two-dimensional 1H,15N and 1H,13C NMR spectra were acquired with harmonized experimental protocols on the unlabeled Fab domain and a uniformly enriched-15N, 20%-13C-enriched system suitability sample derived from the NISTmAb. Chemometric analyses from over 400 spectral maps acquired on 39 different NMR spectrometers ranging from 500 MHz to 900 MHz demonstrate spectral fingerprints that are fit-for-purpose for the assessment of HOS. The 2D-NMR method is shown to provide the measurement reliability needed to move the technique from an emerging technology to a harmonized, routine measurement that can be generally applied with great confidence to high precision assessments of the HOS of mAb-based biotherapeutics. ; ISSN:1942-0862 ; ISSN:1942-0870
BASE
The increased interest in using monoclonal antibodies (mAbs) as a platform for biopharmaceuticals has led to the need for new analytical techniques that can precisely assess physicochemical properties of these large and very complex drugs for the purpose of correctly identifying quality attributes (QA). One QA, higher order structure (HOS), is unique to biopharmaceuticals and essential for establishing consistency in biopharmaceutical manufacturing, detecting process-related variations from manufacturing changes and establishing comparability between biologic products. To address this measurement challenge, two-dimensional nuclear magnetic resonance spectroscopy (2D-NMR) methods were introduced that allow for the precise atomic-level comparison of the HOS between two proteins, including mAbs. Here, an inter-laboratory comparison involving 26 industrial, government and academic laboratories worldwide was performed as a benchmark using the NISTmAb, from the National Institute of Standards and Technology (NIST), to facilitate the translation of the 2D-NMR method into routine use for biopharmaceutical product development. Two-dimensional ¹H,¹⁵N and ¹H,¹³C NMR spectra were acquired with harmonized experimental protocols on the unlabeled Fab domain and a uniformly enriched-¹⁵N, 20%-¹³C-enriched system suitability sample derived from the NISTmAb. Chemometric analyses from over 400 spectral maps acquired on 39 different NMR spectrometers ranging from 500 MHz to 900 MHz demonstrate spectral fingerprints that are fit-for-purpose for the assessment of HOS. The 2D-NMR method is shown to provide the measurement reliability needed to move the technique from an emerging technology to a harmonized, routine measurement that can be generally applied with great confidence to high precision assessments of the HOS of mAb-based biotherapeutics. ; Peer reviewed: Yes ; NRC publication: Yes
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