---
res:
  bibo_abstract:
  - 'Formation of new amyloid fibrils and oligomers from monomeric protein on the
    surfaces of existing fibrils is an important driver of many disorders such as
    Alzheimer’s and Parkinson’s diseases. The structural basis of this secondary nucleation
    process, however, is poorly understood. Here, we ask whether secondary nucleation
    sites are found predominantly at rare growth defects: irregularities in the fibril
    core structure incorporated during their original assembly. We first demonstrate
    using the specific inhibitor of secondary nucleation, Brichos, that secondary
    nucleation sites on Alzheimer’s disease-associated fibrils composed of Aβ40 and
    Aβ42 peptides are rare compared to the number of protein molecules they contain.
    We then grow Aβ40 fibrils under conditions designed to eliminate most growth defects
    while leaving the regular fibril morphology unchanged, and confirm the latter
    using cryo-electron microscopy. We measure both the ability of these annealed
    fibrils to promote secondary nucleation and the stoichiometry of their secondary
    nucleation sites, finding that both are greatly reduced as predicted. Re-analysis
    of published data for other proteins suggests that fibril growth defects may also
    drive secondary nucleation generally across most amyloids. These findings could
    unlock structure-based drug design of therapeutics that aim to halt amyloid disorders
    by inhibiting secondary nucleation sites.@eng'
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Jing
      foaf_name: Hu, Jing
      foaf_surname: Hu
  - foaf_Person:
      foaf_givenName: Tom
      foaf_name: Scheidt, Tom
      foaf_surname: Scheidt
  - foaf_Person:
      foaf_givenName: Dev
      foaf_name: Thacker, Dev
      foaf_surname: Thacker
  - foaf_Person:
      foaf_givenName: Emil
      foaf_name: Axell, Emil
      foaf_surname: Axell
  - foaf_Person:
      foaf_givenName: Elin
      foaf_name: Stemme, Elin
      foaf_surname: Stemme
  - foaf_Person:
      foaf_givenName: Urszula
      foaf_name: Łapińska, Urszula
      foaf_surname: Łapińska
  - foaf_Person:
      foaf_givenName: Stefan
      foaf_name: Wennmalm, Stefan
      foaf_surname: Wennmalm
  - foaf_Person:
      foaf_givenName: Georg
      foaf_name: Meisl, Georg
      foaf_surname: Meisl
  - foaf_Person:
      foaf_givenName: Samo
      foaf_name: Curk, Samo
      foaf_surname: Curk
      foaf_workInfoHomepage: http://www.librecat.org/personId=031eff0d-d481-11ee-8508-cd12a7a86e5b
    orcid: 0000-0001-6160-9766
  - foaf_Person:
      foaf_givenName: Maria
      foaf_name: Andreasen, Maria
      foaf_surname: Andreasen
  - foaf_Person:
      foaf_givenName: Michele
      foaf_name: Vendruscolo, Michele
      foaf_surname: Vendruscolo
  - foaf_Person:
      foaf_givenName: Paolo
      foaf_name: Arosio, Paolo
      foaf_surname: Arosio
  - foaf_Person:
      foaf_givenName: Anđela
      foaf_name: Šarić, Anđela
      foaf_surname: Šarić
      foaf_workInfoHomepage: http://www.librecat.org/personId=bf63d406-f056-11eb-b41d-f263a6566d8b
    orcid: 0000-0002-7854-2139
  - foaf_Person:
      foaf_givenName: Jeremy D.
      foaf_name: Schmit, Jeremy D.
      foaf_surname: Schmit
  - foaf_Person:
      foaf_givenName: Tuomas P.J.
      foaf_name: Knowles, Tuomas P.J.
      foaf_surname: Knowles
  - foaf_Person:
      foaf_givenName: Emma
      foaf_name: Sparr, Emma
      foaf_surname: Sparr
  - foaf_Person:
      foaf_givenName: Sara
      foaf_name: Linse, Sara
      foaf_surname: Linse
  - foaf_Person:
      foaf_givenName: Thomas C.T.
      foaf_name: Michaels, Thomas C.T.
      foaf_surname: Michaels
  - foaf_Person:
      foaf_givenName: Alexander J.
      foaf_name: Dear, Alexander J.
      foaf_surname: Dear
  bibo_doi: 10.1038/s41467-026-69377-1
  bibo_volume: 17
  dct_date: 2026^xs_gYear
  dct_isPartOf:
  - http://id.crossref.org/issn/2041-1723
  dct_language: eng
  dct_publisher: Springer Nature@
  dct_title: Structural defects in amyloid-β fibrils drive secondary nucleation@
  fabio_hasPubmedId: '41708600'
...