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Trodusquemine enhances Aß42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes.
Limbocker, Ryan; Chia, Sean; Ruggeri, Francesco S; Perni, Michele; Cascella, Roberta; Heller, Gabriella T; Meisl, Georg; Mannini, Benedetta; Habchi, Johnny; Michaels, Thomas C T; Challa, Pavan K; Ahn, Minkoo; Casford, Samuel T; Fernando, Nilumi; Xu, Catherine K; Kloss, Nina D; Cohen, Samuel I A; Kumita, Janet R; Cecchi, Cristina; Zasloff, Michael; Linse, Sara; Knowles, Tuomas P J; Chiti, Fabrizio; Vendruscolo, Michele; Dobson, Christopher M.
Afiliação
  • Limbocker R; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Chia S; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Ruggeri FS; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Perni M; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Cascella R; Department of Experimental and Clinical Biomedical Science, University of Florence, Florence, 50134, Italy.
  • Heller GT; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Meisl G; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Mannini B; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Habchi J; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Michaels TCT; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Challa PK; Paulson School of Engineering and Applied Sciences, Harvard University, Cambridge, MA, 02138, USA.
  • Ahn M; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Casford ST; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Fernando N; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Xu CK; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Kloss ND; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Cohen SIA; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Kumita JR; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Cecchi C; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Zasloff M; Department of Experimental and Clinical Biomedical Science, University of Florence, Florence, 50134, Italy.
  • Linse S; MedStar-Georgetown Transplant Institute, Georgetown University School of Medicine, Washington, DC, 20010, USA.
  • Knowles TPJ; Department of Biochemistry and Structural Biology, Lund University, SE221 00, Lund, Sweden.
  • Chiti F; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
  • Vendruscolo M; Cavendish Laboratory, Department of Physics, University of Cambridge, Cambridge, CB3 0HE, UK.
  • Dobson CM; Department of Experimental and Clinical Biomedical Science, University of Florence, Florence, 50134, Italy. fabrizio.chiti@unifi.it.
Nat Commun ; 10(1): 225, 2019 01 15.
Article em En | MEDLINE | ID: mdl-30644384

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fragmentos de Peptídeos / Espermina / Colestanos / Peptídeos beta-Amiloides / Doença de Alzheimer Idioma: En Revista: Nat Commun Ano de publicação: 2019 Tipo de documento: Article País de afiliação: Reino Unido

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fragmentos de Peptídeos / Espermina / Colestanos / Peptídeos beta-Amiloides / Doença de Alzheimer Idioma: En Revista: Nat Commun Ano de publicação: 2019 Tipo de documento: Article País de afiliação: Reino Unido