ArticleProceedings of the National Academy of Sciences of the United States of America1999
De novo amyloid proteins from designed combinatorial libraries.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.
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Who cites it
97 citing papers in PubMed, 324 citations in OpenAlex.
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- Data-mining unveils structure-property-activity correlation of viral infectivity enhancing self-assembling peptides.Nature communications · 2023Article
- The Role of Proteolysis in Amyloidosis.International journal of molecular sciences · 2022Review
- Catalytically Active Amyloids as Future Bionanomaterials.Nanomaterials (Basel, Switzerland) · 2022Review
- An aggregation inhibitor specific to oligomeric intermediates of Aβ42 derived from phage display libraries of stable, small proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- AMYPred-FRL is a novel approach for accurate prediction of amyloid proteins by using feature representation learning.Scientific reports · 2022Article
- Amyloid-like aggregating proteins cause lysosomal defects in neurons via gain-of-function toxicity.Life science alliance · 2022Article
- Deterministic chaos in the self-assembly of β sheet nanotubes from an amphipathic oligopeptide.Matter · 2021Article
- Fluc-EGFP reporter mice reveal differential alterations of neuronal proteostasis in aging and disease.The EMBO journal · 2021Article
- Advanced Methods for the Characterization of Supramolecular Hydrogels.Gels (Basel, Switzerland) · 2021Review
- Catalytic Amyloids as Novel Synthetic Hydrolases.International journal of molecular sciences · 2021Review
- Multiple pathways of toxicity induced byeLife · 2021Article
- Covalent Linkage and Macrocylization Preserve and Enhance Synergistic Interactions in Catalytic Amyloids.Chembiochem : a European journal of chemical biology · 2021Article
- Review
- Harnessing biomolecular condensates in living cells.Journal of biochemistry · 2019Review
- Article
- Protein engineering approaches for antibody fragments: directed evolution and rational design approaches.Turkish journal of biology = Turk biyoloji dergisi · 2019Article
- Amyloid and the origin of life: self-replicating catalytic amyloids as prebiotic informational and protometabolic entities.Cellular and molecular life sciences : CMLS · 2018Article
- Hierarchical design of artificial proteins and complexes toward synthetic structural biology.Biophysical reviews · 2018Review
37 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid deposits are associated with several neurodegenerative diseases, including Alzheimer's disease and the prion diseases. The amyloid fibrils isolated from these different diseases share similar structural features. However, the protein sequences that assemble into these fibrils differ substantially from one disease to another. To probe the relationship between amino acid sequence and the propensity to form amyloid, we studied a combinatorial library of sequences designed de novo. All sequences in the library were designed to share an identical pattern of alternating polar and nonpolar residues, but the precise identities of these side chains were not constrained and were varied combinatorially. The resulting proteins self-assemble into large oligomers visible by electron microscopy as amyloid-like fibrils. Like natural amyloid, the de novo fibrils are composed of beta-sheet secondary structure and bind the diagnostic dye, Congo red. Thus, binary patterning of polar and nonpolar residues arranged in alternating periodicity can direct protein sequences to form fibrils resembling amyloid. The model amyloid fibrils assemble and disassemble reversibly, providing a tractable system for both basic studies into the mechanisms of fibril assembly and the development of molecular therapies that interfere with this assembly.
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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.