Dissecting the functional behavior of the differentially phosphorylated prolyl isomerase, Pin1.

Autor: Kay DF; School of Biosciences, University of Birmingham, Edgbaston, UK., Ozleyen A; Leicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, UK.; School of Chemistry, University of Leicester, Leicester, UK., Heras CML; Leicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, UK.; School of Chemistry, University of Leicester, Leicester, UK., Doveston RG; Leicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, UK.; School of Chemistry, University of Leicester, Leicester, UK., Leney AC; School of Biosciences, University of Birmingham, Edgbaston, UK.

Publikováno v: Protein science : a publication of the Protein Society [Protein Sci] 2024 Sep; Vol. 33 (9), pp. e5138.

Characterizing the protein-protein interaction between MDM2 and 14-3-3σ; proof of concept for small molecule stabilization.

Autor: Ward JA; Leicester Institute for Structural and Chemical Biology, University of Leicester, Leicester, UK; Mechanisms of Cancer and Aging Laboratory, Department of Molecular and Cell Biology, University of Leicester, Leicester, UK., Romartinez-Alonso B; Leicester Institute for Structural and Chemical Biology, University of Leicester, Leicester, UK; Department of Molecular and Cell Biology, University of Leicester, Leicester, UK., Kay DF; School of Biosciences, University of Birmingham, Edgbaston, Birmingham, UK., Bellamy-Carter J; School of Biosciences, University of Birmingham, Edgbaston, Birmingham, UK., Thurairajah B; Leicester Institute for Structural and Chemical Biology, University of Leicester, Leicester, UK; School of Chemistry, University of Leicester, Leicester, UK., Basran J; Department of Molecular and Cell Biology, University of Leicester, Leicester, UK., Kwon H; Leicester Institute for Structural and Chemical Biology, University of Leicester, Leicester, UK; Department of Molecular and Cell Biology, University of Leicester, Leicester, UK., Leney AC; School of Biosciences, University of Birmingham, Edgbaston, Birmingham, UK., Macip S; Mechanisms of Cancer and Aging Laboratory, Department of Molecular and Cell Biology, University of Leicester, Leicester, UK; FoodLab, Faculty of Health Sciences, Universitat Oberta de Catalunya, Barcelona, Spain; Josep Carreras Leukaemia Research Institute, Ctra de Can Ruti, Camí de les Escoles, s/n, Badalona, Barcelona, Spain., Roversi P; Leicester Institute for Structural and Chemical Biology, University of Leicester, Leicester, UK; Institute of Agricultural Biology and Biotechnology, C.N.R., Unit of Milan, Milano, Italy., Muskett FW; Leicester Institute for Structural and Chemical Biology, University of Leicester, Leicester, UK; Department of Molecular and Cell Biology, University of Leicester, Leicester, UK., Doveston RG; Leicester Institute for Structural and Chemical Biology, University of Leicester, Leicester, UK; School of Chemistry, University of Leicester, Leicester, UK. Electronic address: r.g.doveston@leicester.ac.uk.

Publikováno v: The Journal of biological chemistry [J Biol Chem] 2024 Feb; Vol. 300 (2), pp. 105651. Date of Electronic Publication: 2024 Jan 16.

Contemporary biophysical approaches for studying 14-3-3 protein-protein interactions.

Autor: Thurairajah B; Leicester Institute for Structural and Chemical Biology and School of Chemistry, University of Leicester, Leicester, United Kingdom., Hudson AJ; Leicester Institute for Structural and Chemical Biology and School of Chemistry, University of Leicester, Leicester, United Kingdom., Doveston RG; Leicester Institute for Structural and Chemical Biology and School of Chemistry, University of Leicester, Leicester, United Kingdom.

Publikováno v: Frontiers in molecular biosciences [Front Mol Biosci] 2022 Nov 08; Vol. 9, pp. 1043673. Date of Electronic Publication: 2022 Nov 08 (Print Publication: 2022).

Structure-Activity Relationship Studies of Trisubstituted Isoxazoles as Selective Allosteric Ligands for the Retinoic-Acid-Receptor-Related Orphan Receptor γt.

Autor: Meijer FA; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Technische Universiteit Eindhoven, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands., Saris AOWM; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Technische Universiteit Eindhoven, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands., Doveston RG; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Technische Universiteit Eindhoven, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands.; Leicester Institute of Structural and Chemical Biology and School of Chemistry, University of Leicester, University Road, LE1 7RH Leicester, U.K., Oerlemans GJM; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Technische Universiteit Eindhoven, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands., de Vries RMJM; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Technische Universiteit Eindhoven, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands., Somsen BA; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Technische Universiteit Eindhoven, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands., Unger A; Lead Discovery Center GmbH, 44227 Dortmund, Germany., Klebl B; Lead Discovery Center GmbH, 44227 Dortmund, Germany., Ottmann C; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Technische Universiteit Eindhoven, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands., Cossar PJ; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Technische Universiteit Eindhoven, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands., Brunsveld L; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Technische Universiteit Eindhoven, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands.

Publikováno v: Journal of medicinal chemistry [J Med Chem] 2021 Jul 08; Vol. 64 (13), pp. 9238-9258. Date of Electronic Publication: 2021 May 19.

Covalent Occlusion of the RORγt Ligand Binding Pocket Allows Unambiguous Targeting of an Allosteric Site.

Autor: Meijer FA; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Technische Universiteit Eindhoven, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands., van den Oetelaar MCM; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Technische Universiteit Eindhoven, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands., Doveston RG; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Technische Universiteit Eindhoven, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands.; Leicester Institute of Structural and Chemical Biology and School of Chemistry, University of Leicester, University Road, Leicester LE1 7RH, United Kingdom., Sampers ENR; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Technische Universiteit Eindhoven, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands., Brunsveld L; Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute for Complex Molecular Systems, Technische Universiteit Eindhoven, Den Dolech 2, 5612 AZ Eindhoven, The Netherlands.

Publikováno v: ACS medicinal chemistry letters [ACS Med Chem Lett] 2021 Mar 08; Vol. 12 (4), pp. 631-639. Date of Electronic Publication: 2021 Mar 08 (Print Publication: 2021).