ArticleProceedings of the National Academy of Sciences of the United States of America2012
Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- Fungal Hydrophobins: Taxonomic Distribution, Functional Roles, Physicochemical Properties, and Biotechnological Applications.Journal of fungi (Basel, Switzerland) · 2026Review
- Heterologous expression and interfacial activity evaluation of Pleurotus ostreatus hydrophobin Vmh2 mutants in Tremella fuciformis.World journal of microbiology & biotechnology · 2026Article
- High-speed atomic force microscopy reveals a surface-catalyzed elongation mechanism of the fungal functional amyloid hydrophobin RolA.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Amorphous-to-rodlet structural transition governs the interfacial functions ofFrontiers in microbiology · 2026Article
- The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- AlphaFold modeling uncovers global structural features of class I and class II fungal hydrophobins.Protein science : a publication of the Protein Society · 2025Article
- Leveraging structure-informed machine learning for fast steric zipper propensity prediction across whole proteomes.PLoS computational biology · 2025Article
- Protein-mediated stabilization of amphotericin B increases its efficacy against diverse fungal pathogens.Microbiology spectrum · 2025Article
- Structural elucidation of four fungal hydrophobins belonging to classes I and II: Results from Alphafold and accelerated molecular dynamics simulations.Computational and structural biotechnology journal · 2025Article
- Characterizing the amyloid core region of the tumor suppressor protein p16The Journal of biological chemistry · 2024Article
- Article
- Characterization of the structure and self-assembly of two distinct class IB hydrophobins.Applied microbiology and biotechnology · 2022Article
- Identification of Candidate Ice Nucleation Activity (INA) Genes inJournal of fungi (Basel, Switzerland) · 2022Article
- What makes functional amyloids work?Critical reviews in biochemistry and molecular biology · 2022Review
- Review
- Adsorption Kinetics and Self-Assembled Structures of Aspergillus oryzae Hydrophobin RolA on Hydrophobic and Charged Solid Surfaces.Applied and environmental microbiology · 2022Article
- The N-terminal tail of the hydrophobin SC16 is not required for rodlet formation.Scientific reports · 2022Article
- Review
- Hydrophobin HGFI assisted immunobiologic sensor based on a cascaded taper integrated ultra-long-period fiber grating.Biomedical optics express · 2021Article
- Genetically Encodable Scaffolds for Optimizing Enzyme Function.Molecules (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The hydrophobin EAS from the fungus Neurospora crassa forms functional amyloid fibrils called rodlets that facilitate spore formation and dispersal. Self-assembly of EAS into fibrillar rodlets occurs spontaneously at hydrophobic:hydrophilic interfaces and the rodlets further associate laterally to form amphipathic monolayers. We have used site-directed mutagenesis and peptide experiments to identify the region of EAS that drives intermolecular association and formation of the cross-β rodlet structure. Transplanting this region into a nonamyloidogenic hydrophobin enables it to form rodlets. We have also determined the structure and dynamics of an EAS variant with reduced rodlet-forming ability. Taken together, these data allow us to pinpoint the conformational changes that take place when hydrophobins self-assemble at an interface and to propose a model for the amphipathic EAS rodlet structure.
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