---
res:
  bibo_abstract:
  - Biological membranes can dramatically accelerate the aggregation of normally soluble
    protein molecules into amyloid fibrils and alter the fibril morphologies, yet
    the molecular mechanisms through which this accelerated nucleation takes place
    are not yet understood. Here, we develop a coarse-grained model to systematically
    explore the effect that the structural properties of the lipid membrane and the
    nature of protein–membrane interactions have on the nucleation rates of amyloid
    fibrils. We identify two physically distinct nucleation pathways—protein-rich
    and lipid-rich—and quantify how the membrane fluidity and protein–membrane affinity
    control the relative importance of those molecular pathways. We find that the
    membrane’s susceptibility to reshaping and being incorporated into the fibrillar
    aggregates is a key determinant of its ability to promote protein aggregation.
    We then characterize the rates and the free-energy profile associated with this
    heterogeneous nucleation process, in which the surface itself participates in
    the aggregate structure. Finally, we compare quantitatively our data to experiments
    on membrane-catalyzed amyloid aggregation of α-synuclein, a protein implicated
    in Parkinson’s disease that predominately nucleates on membranes. More generally,
    our results provide a framework for understanding macromolecular aggregation on
    lipid membranes in a broad biological and biotechnological context.@eng
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Johannes
      foaf_name: Krausser, Johannes
      foaf_surname: Krausser
  - foaf_Person:
      foaf_givenName: Tuomas P. J.
      foaf_name: Knowles, Tuomas P. J.
      foaf_surname: Knowles
  - 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
  bibo_doi: 10.1073/pnas.2007694117
  bibo_issue: '52'
  bibo_volume: 117
  dct_date: 2020^xs_gYear
  dct_isPartOf:
  - http://id.crossref.org/issn/0027-8424
  - http://id.crossref.org/issn/1091-6490
  dct_language: eng
  dct_publisher: National Academy of Sciences@
  dct_title: Physical mechanisms of amyloid nucleation on fluid membranes@
  fabio_hasPubmedId: '33328273'
...