A refined model for the TSG-6 link module in complex with hyaluronan: use of defined oligosaccharides to probe structure and function

Autor: Higman, VA, Briggs, DC, Mahoney, DJ, Blundell, CD, Sattelle, BM, Dyer, DP, Green, DE, DeAngelis, PL, Almond, A, Milner, CM, Day, AJ

Tumor necrosis factor-stimulated gene-6 (TSG-6) is an inflammation-associated hyaluronan (HA)-binding protein that contributes to remodeling of HA-rich extracellular matrices during inflammatory processes and ovulation. The HA-binding domain of TSG-6

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Perspective: on the importance of extensive, high-quality and reliable deposition of biomolecular NMR data in the age of artificial intelligence.

Autor: Higman VA; Department of Molecular and Cell Biology, Leicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, LE1 7RH, UK. vad5@leicester.ac.uk., Płoskoń E; Department of Molecular and Cell Biology, Leicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, LE1 7RH, UK., Thompson GS; Wellcome Trust Biological NMR Facility, School of Biosciences, Division of Natural Sciences, University of Kent, Canterbury, Kent, CT2 7NZ, UK., Vuister GW; Department of Molecular and Cell Biology, Leicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, LE1 7RH, UK.

Publikováno v: Journal of biomolecular NMR [J Biomol NMR] 2024 Dec; Vol. 78 (4), pp. 193-197. Date of Electronic Publication: 2024 Oct 20.

The streptococcal multidomain fibrillar adhesin CshA has an elongated polymeric architecture.

Autor: Back CR; Bristol Dental School, University of Bristol, Bristol BS1 2LY, United Kingdom.; School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom.; BrisSynBio Synthetic Biology Research Centre, University of Bristol, Bristol BS8 1TQ, United Kingdom., Higman VA; School of Chemistry, University of Bristol, Bristol BS8 1TS, United Kingdom., Le Vay K; School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom.; Bristol Centre for Functional Nanomaterials, H. H. Wills Physics Laboratory, University of Bristol, Bristol BS8 1TL, United Kingdom., Patel VV; School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom., Parnell AE; School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom.; BrisSynBio Synthetic Biology Research Centre, University of Bristol, Bristol BS8 1TQ, United Kingdom., Frankel D; School of Engineering, Newcastle University, Newcastle-upon-Tyne NE1 7RU, United Kingdom., Jenkinson HF; Bristol Dental School, University of Bristol, Bristol BS1 2LY, United Kingdom., Burston SG; School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom.; BrisSynBio Synthetic Biology Research Centre, University of Bristol, Bristol BS8 1TQ, United Kingdom., Crump MP; BrisSynBio Synthetic Biology Research Centre, University of Bristol, Bristol BS8 1TQ, United Kingdom.; School of Chemistry, University of Bristol, Bristol BS8 1TS, United Kingdom., Nobbs AH; Bristol Dental School, University of Bristol, Bristol BS1 2LY, United Kingdom Angela.Nobbs@bristol.ac.uk., Race PR; School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom Paul.Race@bristol.ac.uk.; BrisSynBio Synthetic Biology Research Centre, University of Bristol, Bristol BS8 1TQ, United Kingdom.

Publikováno v: The Journal of biological chemistry [J Biol Chem] 2020 May 08; Vol. 295 (19), pp. 6689-6699. Date of Electronic Publication: 2020 Mar 30.

The structural basis for dynamic DNA binding and bridging interactions which condense the bacterial centromere.

Autor: Fisher GL; DNA:protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol, United Kingdom., Pastrana CL; Department of Macromolecular Structures, Centro Nacional de Biotecnologia, Consejo Superior de Investigaciones Cientificas, Madrid, Spain., Higman VA; School of Chemistry, University of Bristol, Bristol, United Kingdom., Koh A; Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle, United Kingdom., Taylor JA; DNA:protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol, United Kingdom., Butterer A; Biomolecular and Analytical Mass Spectrometry Group, Department of Chemistry, University of Antwerp, Antwerpen, Belgium., Craggs T; Department of Chemistry, University of Sheffield, Sheffield, United Kingdom., Sobott F; Biomolecular and Analytical Mass Spectrometry Group, Department of Chemistry, University of Antwerp, Antwerpen, Belgium.; Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom.; School of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom., Murray H; Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle, United Kingdom., Crump MP; School of Chemistry, University of Bristol, Bristol, United Kingdom., Moreno-Herrero F; Department of Macromolecular Structures, Centro Nacional de Biotecnologia, Consejo Superior de Investigaciones Cientificas, Madrid, Spain., Dillingham MS; DNA:protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol, United Kingdom.

Publikováno v: ELife [Elife] 2017 Dec 15; Vol. 6. Date of Electronic Publication: 2017 Dec 15.