ArticleBiophysical journal2011
Physical properties of polymorphic yeast prion amyloid fibers.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 0 citations in OpenAlex.
- Single-Molecule Insight Into α-Synuclein Fibril Structure and Mechanics Modulated by Chemical Compounds.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Single-molecule investigations of single-chain cellulose biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Amyloid fibril length distribution from dynamic light scattering data.European biophysics journal : EBJ · 2022Article
- Amyloid fibrils embodying distinctive yeast prion phenotypes exhibit diverse morphologies.FEMS yeast research · 2018Article
- Real-time magnetic actuation of DNA nanodevices via modular integration with stiff micro-levers.Nature communications · 2018Article
- Mapping the Broad Structural and Mechanical Properties of Amyloid Fibrils.Biophysical journal · 2017Article
- Pre-T Cell Receptors (Pre-TCRs) Leverage Vβ Complementarity Determining Regions (CDRs) and Hydrophobic Patch in Mechanosensing Thymic Self-ligands.The Journal of biological chemistry · 2016Article
- Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion.Frontiers in molecular neuroscience · 2016Article
- Orientation of aromatic residues in amyloid cores: structural insights into prion fiber diversity.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Prions in yeast.Genetics · 2012Review
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Amyloid fibers play important roles in many human diseases and natural biological processes and have immense potential as novel nanomaterials. We explore the physical properties of polymorphic amyloid fibers formed by yeast prion protein Sup35. Amyloid fibers that conferred distinct prion phenotypes ([PSI(+)]), strong (S) versus weak (W) nonsense suppression, displayed different physical properties. Both S[PSI(+)] and W[PSI(+)] fibers contained structural inhomogeneities, specifically local regions of static curvature in S[PSI(+)] fibers and kinks and self-cross-linking in W[PSI(+)] fibers. Force-extension experiments with optical tweezers revealed persistence lengths of 1.5 μm and 3.3 μm and axial stiffness of 5600 pN and 9100 pN for S[PSI(+)] and W[PSI(+)] fibers, respectively. Thermal fluctuation analysis confirmed the twofold difference in persistence length between S[PSI(+)] and W[PSI(+)] fibers and revealed a torsional stiffness of kinks and cross-links of ~100-200 pN·nm/rad.
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Registered trials
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