ArticleProceedings of the National Academy of Sciences of the United States of America2012
Intrinsic disorder modulates protein self-assembly and aggregation.
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 45 papers.
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Who cites it
45 citing papers in PubMed.
- Reverse-engineering amyloid strains with generative protein design.bioRxiv : the preprint server for biology · 2026Article
- AlphaFold modeling uncovers global structural features of class I and class II fungal hydrophobins.Protein science : a publication of the Protein Society · 2025Article
- Co-translational ribosome pairing enables native assembly of misfolding-prone subunits.Nature communications · 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
- Production of Distinct Fibrillar, Oligomeric, and Other Aggregation States from Network Models of Multibody Interaction.Journal of chemical theory and computation · 2024Article
- Self-Assembly of Polymers and Their Applications in the Fields of Biomedicine and Materials.Polymers · 2024Review
- Using NMR diffusion data to validate MD models of disordered proteins: Test case of N-terminal tail of histone H4.Biophysical journal · 2024Article
- Modeling the effects of phosphorylation on phase separation of the FUS low-complexity domain.Biophysical journal · 2023Article
- Structure and diffusive dynamics of aspartate α-decarboxylase (ADC) liganded with D-serine in aqueous solution.Physical chemistry chemical physics : PCCP · 2022Article
- Proteome-wide landscape of solubility limits in a bacterial cell.Scientific reports · 2022Article
- The Role of Cyclodextrins against Interface-Induced Denaturation in Pharmaceutical Formulations: A Molecular Dynamics Approach.Molecular pharmaceutics · 2021Article
- Article
- Effect of the air-water interface on the conformation of amyloid beta.Biointerphases · 2020Article
- MEF2 impairment underlies skeletal muscle atrophy in polyglutamine disease.Acta neuropathologica · 2020Article
- Amyloid structures: much more than just a cross-β fold.Current opinion in structural biology · 2020Review
- The first year.Acta neuropathologica · 2020Article
- Botcinic acid biosynthesis in Botrytis cinerea relies on a subtelomeric gene cluster surrounded by relics of transposons and is regulated by the ZnCurrent genetics · 2019Article
- LOXL1 folding in exfoliation glaucoma.Advances in protein chemistry and structural biology · 2019Review
- The structural basis of nanobody unfolding reversibility and thermoresistance.Scientific reports · 2018Article
- Oligomerization Alters Binding Affinity Between Amyloid Beta and a Modulator of Peptide Aggregation.The journal of physical chemistry. C, Nanomaterials and interfaces · 2017Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Protein molecules have evolved to adopt distinctive and well-defined functional and soluble states under physiological conditions. In some circumstances, however, proteins can self-assemble into fibrillar aggregates designated as amyloid fibrils. In vivo these processes are normally associated with severe pathological conditions but can sometimes have functional relevance. One such example is the hydrophobins, whose aggregation at air-water interfaces serves to create robust protein coats that help fungal spores to resist wetting and thus facilitate their dispersal in the air. We have performed multiscale simulations to address the molecular determinants governing the formation of functional amyloids by the class I fungal hydrophobin EAS. Extensive samplings of full-atom replica-exchange molecular dynamics and coarse-grained simulations have allowed us to identify factors that distinguish aggregation-prone from highly soluble states of EAS. As a result of unfavourable entropic terms, highly dynamical regions are shown to exert a crucial influence on the propensity of the protein to aggregate under different conditions. More generally, our findings suggest a key role that specific flexible structural elements can play to ensure the existence of soluble and functional states of proteins under physiological conditions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.