Molecular mechanisms of fibrillogenesis and the protective role of amyloid P component: two possible avenues for therapy

Autor: Mb, Pepys, Ga, Tennent, Dr, Booth, Bellotti V, Laurence Lovat, Sy, Tan, Persey MR, Wl, Hutchinson, Se, Booth, Madhoo S, Ak, Soutar, Pn, Hawkins, Van Zyl-Smit R, Jm, Campistol, Pe, Fraser, Se, Radford, Cv, Robinson, Sunde M, Lc, Serpell, Cc, Blake

Publikováno v: Europe PubMed Central

Amyloid deposits regress when the supply of fibril precursor proteins is sufficiently reduced, indicating that amyloid fibrils are degradable in vivo. Serum amyloid P component (SAP), a universal constituent of amyloid deposits, efficiently protects

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::01e3af960530a2a6a66565f0ac41982f
https://pubmed.ncbi.nlm.nih.gov/8915605

Expanding the Protein Universe.

Autor: Serpell LC; Sussex Neuroscience, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, UK., Otzen DE; Interdisciplinary Nanoscience Centre (iNANO), Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark. Electronic address: dao@inano.au.dk., Radford SE; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, UK. Electronic address: S.e.radford@leeds.ac.uk.

Publikováno v: Journal of molecular biology [J Mol Biol] 2024 Nov 01; Vol. 436 (21), pp. 168812. Date of Electronic Publication: 2024 Oct 04.

Outer membrane protein assembly mediated by BAM-SurA complexes.

Autor: Fenn KL; Astbury Centre for Structural Molecular Biology and School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK., Horne JE; Astbury Centre for Structural Molecular Biology and School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.; Department of Biochemistry, Tennis Court Road, Cambridge, CB2 1GA, UK., Crossley JA; Astbury Centre for Structural Molecular Biology and School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK., Böhringer N; Institute for Insect Biotechnology, Justus-Liebig-University Giessen, 35392, Giessen, Germany.; German Center for Infection Research (DZIF), Partner Site Giessen-Marburg-Langen, 35392, Giessen, Germany.; Branch for Bioresources, Fraunhofer Institute for Molecular Biology and Applied Ecology (IME), 35392, Giessen, Germany., Horne RJ; Astbury Centre for Structural Molecular Biology and School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.; Steinmetz Building, Granta Park, Great Abington, Cambridge, CB21 6DG, UK., Schäberle TF; Institute for Insect Biotechnology, Justus-Liebig-University Giessen, 35392, Giessen, Germany.; German Center for Infection Research (DZIF), Partner Site Giessen-Marburg-Langen, 35392, Giessen, Germany.; Branch for Bioresources, Fraunhofer Institute for Molecular Biology and Applied Ecology (IME), 35392, Giessen, Germany., Calabrese AN; Astbury Centre for Structural Molecular Biology and School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK., Radford SE; Astbury Centre for Structural Molecular Biology and School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK. s.e.radford@leeds.ac.uk., Ranson NA; Astbury Centre for Structural Molecular Biology and School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK. n.a.ranson@leeds.ac.uk.

Publikováno v: Nature communications [Nat Commun] 2024 Sep 01; Vol. 15 (1), pp. 7612. Date of Electronic Publication: 2024 Sep 01.

Sculpting conducting nanopore size and shape through de novo protein design.

Autor: Berhanu S; Department of Biochemistry, The University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA., Majumder S; Department of Biochemistry, The University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA., Müntener T; Biozentrum, University of Basel, Basel, Switzerland., Whitehouse J; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT., Berner C; Structural Biology Brussel, Vrije Universiteit Brussel, Brussels, Belgium.; VUB-VIB Center for Structural Biology, Brussels, Belgium., Bera AK; Department of Biochemistry, The University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA., Kang A; Department of Biochemistry, The University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA., Liang B; Department of Molecular Physiology and Biological Physics and Center for Membrane and Cell Physiology, University of Virginia, Charlottesville, VA, USA., Khan N; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT., Sankaran B; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA., Tamm LK; Department of Molecular Physiology and Biological Physics and Center for Membrane and Cell Physiology, University of Virginia, Charlottesville, VA, USA., Brockwell DJ; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT., Hiller S; Biozentrum, University of Basel, Basel, Switzerland., Radford SE; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT., Baker D; Department of Biochemistry, The University of Washington, Seattle, WA, USA.; Institute for Protein Design, University of Washington, Seattle, WA, USA.; Howard Hughes Medical Institute, University of Washington, Seattle, WA, USA., Vorobieva AA; Structural Biology Brussel, Vrije Universiteit Brussel, Brussels, Belgium.; VUB-VIB Center for Structural Biology, Brussels, Belgium.; VIB Center for AI and Computational Biology, Belgium.

Publikováno v: Science (New York, N.Y.) [Science] 2024 Jul 19; Vol. 385 (6706), pp. 282-288. Date of Electronic Publication: 2024 Jul 18.

A Potent Sybody Selectively Inhibits α-Synuclein Amyloid Formation by Binding to the P1 Region.

Autor: Gialama D; Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, London W12 0BZ, U.K., Vadukul DM; Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, London W12 0BZ, U.K., Thrush RJ; Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, London W12 0BZ, U.K.; Institute of Chemical Biology, Molecular Sciences Research Hub, Imperial College London, London W12 0BZ, U.K., Radford SE; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, U.K., Aprile FA; Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, London W12 0BZ, U.K.; Institute of Chemical Biology, Molecular Sciences Research Hub, Imperial College London, London W12 0BZ, U.K.

Publikováno v: Journal of medicinal chemistry [J Med Chem] 2024 Jun 27; Vol. 67 (12), pp. 9857-9868. Date of Electronic Publication: 2024 Jun 06.