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  • Limbocker, RyanUniversity of Cambridge (author)

Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes

  • Article/chapterEnglish2019

Publisher, publication year, extent ...

  • 2019-01-15
  • Springer Science and Business Media LLC,2019

Numbers

  • LIBRIS-ID:oai:lup.lub.lu.se:feaa2c3c-33e4-40d3-bfb2-e6edaa2233b1
  • https://lup.lub.lu.se/record/feaa2c3c-33e4-40d3-bfb2-e6edaa2233b1URI
  • https://doi.org/10.1038/s41467-018-07699-5DOI

Supplementary language notes

  • Language:English
  • Summary in:English

Part of subdatabase

Classification

  • Subject category:art swepub-publicationtype
  • Subject category:ref swepub-contenttype

Notes

  • Transient oligomeric species formed during the aggregation process of the 42-residue form of the amyloid-β peptide (Aβ42) are key pathogenic agents in Alzheimer’s disease (AD). To investigate the relationship between Aβ42 aggregation and its cytotoxicity and the influence of a potential drug on both phenomena, we have studied the effects of trodusquemine. This aminosterol enhances the rate of aggregation by promoting monomer-dependent secondary nucleation, but significantly reduces the toxicity of the resulting oligomers to neuroblastoma cells by inhibiting their binding to the cellular membranes. When administered to a C. elegans model of AD, we again observe an increase in aggregate formation alongside the suppression of Aβ42-induced toxicity. In addition to oligomer displacement, the reduced toxicity could also point towards an increased rate of conversion of oligomers to less toxic fibrils. The ability of a small molecule to reduce the toxicity of oligomeric species represents a potential therapeutic strategy against AD.

Subject headings and genre

Added entries (persons, corporate bodies, meetings, titles ...)

  • Chia, SeanUniversity of Cambridge (author)
  • Ruggeri, Francesco S.University of Cambridge (author)
  • Perni, MicheleUniversity of Cambridge (author)
  • Cascella, RobertaUniversity of Florence (author)
  • Heller, Gabriella T.University of Cambridge (author)
  • Meisl, GeorgUniversity of Cambridge (author)
  • Mannini, BenedettaUniversity of Cambridge (author)
  • Habchi, JohnnyUniversity of Cambridge (author)
  • Michaels, Thomas C.T.University of Cambridge,Harvard University (author)
  • Challa, Pavan K.University of Cambridge (author)
  • Ahn, MinkooUniversity of Cambridge (author)
  • Casford, Samuel T.University of Cambridge (author)
  • Fernando, NilumiUniversity of Cambridge (author)
  • Xu, Catherine K.University of Cambridge (author)
  • Kloss, Nina D.University of Cambridge (author)
  • Cohen, Samuel I.A.University of Cambridge (author)
  • Kumita, Janet R.University of Cambridge (author)
  • Cecchi, CristinaUniversity of Florence (author)
  • Zasloff, MichaelGeorgetown University (author)
  • Linse, SaraLund University,Lunds universitet,NanoLund: Centre for Nanoscience,Annan verksamhet, LTH,Lunds Tekniska Högskola,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Other operations, LTH,Faculty of Engineering, LTH,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)fkm2-sli (author)
  • Knowles, Tuomas P.J.University of Cambridge (author)
  • Chiti, FabrizioUniversity of Florence (author)
  • Vendruscolo, MicheleUniversity of Cambridge (author)
  • Dobson, Christopher M.University of Cambridge (author)
  • University of CambridgeUniversity of Florence (creator_code:org_t)

Related titles

  • In:Nature Communications: Springer Science and Business Media LLC10:12041-1723

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