ArticleNature structural & molecular biology2010
Optical trapping with high forces reveals unexpected behaviors of prion fibrils.
Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Single-Molecule Insight Into α-Synuclein Fibril Structure and Mechanics Modulated by Chemical Compounds.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Myosin II Adjusts Motility Properties and Regulates Force Production Based on Motor Environment.Cellular and molecular bioengineering · 2022Article
- Stability matters, too - the thermodynamics of amyloid fibril formation.Chemical science · 2022Review
- Article
- Amyloid fibrils embodying distinctive yeast prion phenotypes exhibit diverse morphologies.FEMS yeast research · 2018Article
- Mechanical Deformation Mechanisms and Properties of Prion Fibrils Probed by Atomistic Simulations.Nanoscale research letters · 2017Article
- Trapping and manipulation of nanoparticles using multifocal optical vortex metalens.Scientific reports · 2017Article
- A dominant-negative mutant inhibits multiple prion variants through a common mechanism.PLoS genetics · 2017Article
- Heparin acts as a structural component of β-endorphin amyloid fibrils rather than a simple aggregation promoter.Chemical communications (Cambridge, England) · 2017Article
- Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo.PLoS genetics · 2016Article
- A Decentralized Approach to the Formulation of Hypotheses: A Hierarchical Structural Model for a Prion Self-Assembled System.Scientific reports · 2016Article
- Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein.Nature communications · 2016Article
- Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.Journal of molecular biology · 2016Review
- Force generation by the growth of amyloid aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A Single-Strand Annealing Protein Clamps DNA to Detect and Secure Homology.PLoS biology · 2015Article
- Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates.PloS one · 2015Article
- Locating folds of the in-register parallel β-sheet of the Sup35p prion domain infectious amyloid.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Article
- Mechanisms of cellular proteostasis: insights from single-molecule approaches.Annual review of biophysics · 2014Review
- Diverse metastable structures formed by small oligomers of α-synuclein probed by force spectroscopy.PloS one · 2014Article
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Authors and funding
5 authors.
Funding
Abstract
Amyloid fibrils are important in diverse cellular functions, feature in many human diseases and have potential applications in nanotechnology. Here we describe methods that combine optical trapping and fluorescent imaging to characterize the forces that govern the integrity of amyloid fibrils formed by a yeast prion protein. A crucial advance was to use the self-templating properties of amyloidogenic proteins to tether prion fibrils, enabling their manipulation in the optical trap. At normal pulling forces the fibrils were impervious to disruption. At much higher forces (up to 250 pN), discontinuities occurred in force-extension traces before fibril rupture. Experiments with selective amyloid-disrupting agents and mutations demonstrated that such discontinuities were caused by the unfolding of individual subdomains. Thus, our results reveal unusually strong noncovalent intermolecular contacts that maintain fibril integrity even when individual monomers partially unfold and extend fibril length.
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