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David Briggs

Researcher at Francis Crick Institute

Publications -  79
Citations -  2540

David Briggs is an academic researcher from Francis Crick Institute. The author has contributed to research in topics: Medicine & Chemistry. The author has an hindex of 30, co-authored 73 publications receiving 2201 citations. Previous affiliations of David Briggs include Manchester Academic Health Science Centre & London Research Institute.

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The Inflammation-associated Protein TSG-6 Cross-links Hyaluronan via Hyaluronan-induced TSG-6 Oligomers

TL;DR: It is found that full-length TSG-6 binds with pronounced positive cooperativity and can cross-link HA at physiologically relevant concentrations, and it is proposed that condensation is the result of protein-mediated HA cross-linking.
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Mapping for Wheelchair Users: Route Navigation in Urban Spaces

TL;DR: A Geographical Information Systems (GIS) network model for the creation of accessibility maps for wheelchair users is developed, providing a tool suitable to assist wheelchair users new to an area; to enable better navigation for existing users; and a means for planners to consider the way in which access is restricted for wheelchair Users in their designs for more inclusive urban environments.
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Comparison of land-use regression models between Great Britain and the Netherlands

TL;DR: In this paper, the authors compared land-use regression models for NO 2 and PM 10, developed with a consistent protocol in Great Britain (GB) and the Netherlands (NL), and found that the performance of models based upon common data was only slightly worse than models optimised with local data.
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Modelling Access with GIS in Urban Systems (MAGUS): capturing the experiences of wheelchair users

TL;DR: This model acts both as a navigational device for wheelchairs users 2013 enabling them to make informed route choices through urban places and as a decision support and planning tool for urban planners 2013 making visible the ways in which built environments are often distorted and hostile spaces for wheelchair users.
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The angiogenic inhibitor long pentraxin PTX3 forms an asymmetric octamer with two binding sites for FGF2.

TL;DR: Biophysical analyses reveal that PTX3 is composed of eight identical protomers, associated through disulfide bonds, forming an elongated and asymmetric, molecule with two differently sized domains interconnected by a stalk, explaining both its quaternary organization and how this is required for its antiangiogenic function.