ArticleNature communications2022
Mapping the sequence specificity of heterotypic amyloid interactions enables the identification of aggregation modifiers.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 24 citations in OpenAlex.
- An N-terminal ATTR Fibril Segment Promotes Transthyretin Amyloid Nucleation and Polymorphism.bioRxiv : the preprint server for biology · 2026Article
- TAF15 amyloids propagate via defined motifs in a prion-like fashion.Nature communications · 2026Article
- A functional amyloid scaffold shapes insect egg coats.bioRxiv : the preprint server for biology · 2026Article
- Reverse-engineering amyloid strains with generative protein design.bioRxiv : the preprint server for biology · 2026Article
- Atomic structures of medin and Aβ fibrils reveal polymorphic remodeling in mixed amyloid systems.Nature communications · 2026Article
- Phagocytes as Plaque Catalysts: Human Macrophages Actively Generate Pathogenic Aβ42 Fibrils with Seeding and Cross-Seeding Potency.bioRxiv : the preprint server for biology · 2025Article
- Medin drives Aβ40 to adopt Aβ42-like fibril polymorphs in vitro.bioRxiv : the preprint server for biology · 2025Article
- Biophysical Studies of Amyloid-Binding Fluorophores to Tau AD Core Fibrils Formed without Cofactors.International journal of molecular sciences · 2024Article
- Production of Distinct Fibrillar, Oligomeric, and Other Aggregation States from Network Models of Multibody Interaction.Journal of chemical theory and computation · 2024Article
- Heterotypic Seeding Generates Mixed Amyloid Polymorphs.Small science · 2024Article
- Heterotypic Seeding Generates Mixed Amyloid Polymorphs.bioRxiv : the preprint server for biology · 2024Article
- Local structural preferences in shaping tau amyloid polymorphism.Nature communications · 2024Article
- PACT - Prediction of amyloid cross-interaction by threading.Scientific reports · 2023Article
- Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023Review
- MAP2 caps tau fibrils and inhibits aggregation.The Journal of biological chemistry · 2023Article
- Enhanced therapeutic window for antimicrobial Pept-ins by investigating their structure-activity relationship.PloS one · 2023Article
- Functional Bacterial Amyloids: Understanding Fibrillation, Regulating Biofilm Fibril Formation and Organizing Surface Assemblies.Molecules (Basel, Switzerland) · 2022Review
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Authors and funding
13 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heterotypic amyloid interactions between related protein sequences have been observed in functional and disease amyloids. While sequence homology seems to favour heterotypic amyloid interactions, we have no systematic understanding of the structural rules determining such interactions nor whether they inhibit or facilitate amyloid assembly. Using structure-based thermodynamic calculations and extensive experimental validation, we performed a comprehensive exploration of the defining role of sequence promiscuity in amyloid interactions. Using tau as a model system we demonstrate that proteins with local sequence homology to tau amyloid nucleating regions can modify fibril nucleation, morphology, assembly and spreading of aggregates in cultured cells. Depending on the type of mutation such interactions inhibit or promote aggregation in a manner that can be predicted from structure. We find that these heterotypic amyloid interactions can result in the subcellular mis-localisation of these proteins. Moreover, equilibrium studies indicate that the critical concentration of aggregation is altered by heterotypic interactions. Our findings suggest a structural mechanism by which the proteomic background can modulate the aggregation propensity of amyloidogenic proteins and we discuss how such sequence-specific proteostatic perturbations could contribute to the selective cellular susceptibility of amyloid disease progression.
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