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

Generation of an induced pluripotent stem cell line (BIORTCi001-A) from a healthy adult indigenous Nigerian participant.

Autor: Muhammad Z; Sussex Neuroscience, School of Life Sciences, University of Sussex, Brighton, UK; Biomedical Science Research and Training Centre, Yobe State University, Damaturu, Yobe State, Nigeria; Department of Human Physiology, College of Medical Sciences, Yobe State University, Damaturu, Yobe State, Nigeria., Brown PW; Sussex Neuroscience, School of Life Sciences, University of Sussex, Brighton, UK., Babazau L; Biomedical Science Research and Training Centre, Yobe State University, Damaturu, Yobe State, Nigeria; Yobe State University Teaching Hospital Damaturu, Yobe State, Nigeria., Alkhamis AI; Biomedical Science Research and Training Centre, Yobe State University, Damaturu, Yobe State, Nigeria; Department of Human Physiology, College of Medical Sciences, Yobe State University, Damaturu, Yobe State, Nigeria; Department of Human Physiology, Faculty of Basic Medical Sciences, Ahmadu Bello University, Zaria, Kaduna State, Nigeria., Goni BW; Biomedical Science Research and Training Centre, Yobe State University, Damaturu, Yobe State, Nigeria; Yobe State University Teaching Hospital Damaturu, Yobe State, Nigeria; Department of Medicine, College of Medical Sciences, University of Maiduguri, Maiduguri, Borno State, Nigeria., Nggada HA; Department of Human Pathology, University of Maiduguri, Maiduguri, Borno State, Nigeria., Mbaya KM; Department of Surgery, University of Maiduguri Teaching Hospital, Maiduguri, Borno State, Nigeria., Wray S; Department of Neurodegenerative Disease, University College London Queen Square Institute of Neurology, London, UK., Marte IH; Department of Pharmacology and Toxicology, Faculty of Pharmacy, University of Maiduguri, Maiduguri, Borno State, Nigeria., Karch CM; Department of Psychiatry and Knight Alzheimer Disease Research Center, Washington University in St Louis, St Louis, MO, USA., Serpell LC; Biomedical Science Research and Training Centre, Yobe State University, Damaturu, Yobe State, Nigeria., Maina MB; Sussex Neuroscience, School of Life Sciences, University of Sussex, Brighton, UK; Biomedical Science Research and Training Centre, Yobe State University, Damaturu, Yobe State, Nigeria. Electronic address: mahmoud.maina@biortc.com.

Publikováno v: Stem cell research [Stem Cell Res] 2024 Oct; Vol. 80, pp. 103503. Date of Electronic Publication: 2024 Jul 20.

Molecular organization of fibroin heavy chain and mechanism of fibre formation in Bombyx mori.

Autor: Moreno-Tortolero RO; School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK. ro.morenotortolero@bristol.ac.uk.; Max Planck-Bristol Centre for Minimal Biology, University of Bristol, Bristol, BS8 1TS, UK. ro.morenotortolero@bristol.ac.uk., Luo Y; School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK.; School of Biochemistry, University of Bristol, University Walk, Bristol, BS8 1TD, UK., Parmeggiani F; School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK.; School of Biochemistry, University of Bristol, University Walk, Bristol, BS8 1TD, UK.; School of Pharmacy and Pharmaceutical Sciences, Cardiff University, Redwood Building, King Edward VII Ave, Cardiff, CF10 3NB, UK., Skaer N; Orthox Ltd, Milton Park, 66 Innovation Drive, Abingdon, OX14 4RQ, UK., Walker R; Orthox Ltd, Milton Park, 66 Innovation Drive, Abingdon, OX14 4RQ, UK., Serpell LC; Sussex Neuroscience, School of Life Sciences, University of Sussex, Brighton, BN1 9QG, UK., Holland C; Department of Materials Science and Engineering, University of Sheffield, Mappin Street, Sheffield, S1 3JD, UK., Davis SA; School of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK. s.a.davis@bristol.ac.uk.

Publikováno v: Communications biology [Commun Biol] 2024 Jun 29; Vol. 7 (1), pp. 786. Date of Electronic Publication: 2024 Jun 29.

Correlative cryo-soft X-ray tomography and cryo-structured illumination microscopy reveal changes to lysosomes in amyloid-β-treated neurons.

Autor: Marshall KE; Sussex Neuroscience, School of Life Sciences, University of Sussex, Falmer, BN1 9QG Brighton, UK. Electronic address: k.e.marshall@sussex.ac.uk., Mengham K; Sussex Neuroscience, School of Life Sciences, University of Sussex, Falmer, BN1 9QG Brighton, UK., Spink MC; Diamond Light Source, Diamond House, Harwell Science and Innovation Campus, Fermi Avenue, OX11 0DE Didcot, UK., Vania L; Sussex Neuroscience, School of Life Sciences, University of Sussex, Falmer, BN1 9QG Brighton, UK., Pollard HJ; Sussex Neuroscience, School of Life Sciences, University of Sussex, Falmer, BN1 9QG Brighton, UK., Darrow MC; Diamond Light Source, Diamond House, Harwell Science and Innovation Campus, Fermi Avenue, OX11 0DE Didcot, UK., Duke E; Diamond Light Source, Diamond House, Harwell Science and Innovation Campus, Fermi Avenue, OX11 0DE Didcot, UK., Harkiolaki M; Diamond Light Source, Diamond House, Harwell Science and Innovation Campus, Fermi Avenue, OX11 0DE Didcot, UK., Serpell LC; Sussex Neuroscience, School of Life Sciences, University of Sussex, Falmer, BN1 9QG Brighton, UK. Electronic address: l.c.serpell@sussex.ac.uk.

Publikováno v: Structure (London, England : 1993) [Structure] 2024 May 02; Vol. 32 (5), pp. 585-593.e3. Date of Electronic Publication: 2024 Mar 11.

Corrigendum: The disease associated Tau35 fragment has an increased propensity to aggregate compared to full-length tau.

Autor: Lyu C; Department of Basic and Clinical Neuroscience, King's College London, London, United Kingdom., Da Vela S; European Molecular Biology Laboratory, Hamburg Site, Hamburg, Germany., Al-Hilaly Y; Sussex Neuroscience, School of Life Sciences, University of Sussex, Brighton, United Kingdom., Marshall KE; Sussex Neuroscience, School of Life Sciences, University of Sussex, Brighton, United Kingdom., Thorogate R; London Centre for Nanotechnology, University College London, London, United Kingdom., Svergun D; European Molecular Biology Laboratory, Hamburg Site, Hamburg, Germany., Serpell LC; Sussex Neuroscience, School of Life Sciences, University of Sussex, Brighton, United Kingdom., Pastore A; Department of Basic and Clinical Neuroscience, King's College London, London, United Kingdom., Hanger DP; Department of Basic and Clinical Neuroscience, King's College London, London, United Kingdom.

Publikováno v: Frontiers in molecular biosciences [Front Mol Biosci] 2023 Sep 15; Vol. 10, pp. 1276677. Date of Electronic Publication: 2023 Sep 15 (Print Publication: 2023).