Author

F. A. Aprile

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 4 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Organism:C. elegans· 1 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

D. M. Vadukul· 3 shared R. J. Thrush· 2 shared A. De Simone· 1 shared A. Huyghebaert· 1 shared A. Masoura· 1 shared B. Mannini· 1 shared C. Camilloni· 1 shared C. M. Dobson· 1 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 13 mutual co-author links

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3 shared papersBiochemistry

D. M. Vadukul

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

The ALS/FTD-related C9orf72 hexanucleotide repeat expansion forms RNA condensates through multimolecular G-quadruplexes

F. Raguseo, A. Huyghebaert, J. Li, R. Balendra, m. Petric Howe, Y. Wang, D. M. Vadukul, D. Tanase, T. E. Maher, L. Malouf, R. Rubio Sanchez, F. A. Aprile, Y. Elani, R. Patani, L. Di Michele, M. Di Antonio

This study shows that C9orf72 hexanucleotide repeat expansions form RNA condensates via multimolecular G-quadruplexes, suggesting a therapeutic target for ALS/FTD.

bioRxiv · Jan 31, 2023Biochemistry

α-Synuclein Aggregation is Triggered by Amyloid-β Oligomers via Heterogeneous Primary Nucleation

D. M. Vadukul, M. Papp, R. J. Thrush, J. Wang, Y. Jin, P. Arosio, F. A. Aprile

This study shows that soluble amyloid-β oligomers trigger α-synuclein aggregation via heterogeneous primary nucleation, forming fibrils with α-synuclein cores and associated amyloid-β.

bioRxiv · Jun 20, 2022Biochemistry

A Facile Method to Produce N-Terminally Truncated α-Synuclein

R. J. Thrush, D. M. Vadukul, F. A. Aprile

This paper presents a method to produce N-terminally truncated α-synuclein without extra terminal residues, revealing the first six residues' role in amyloid formation.

bioRxiv · Feb 21, 2022Biochemistry

A Chemical Mutagenesis Approach to Insert Post-Translational Modifications in Aggregation-Prone Proteins

Y. Ge, A. Masoura, J. Yang, F. A. Aprile

The paper introduces a method to maintain amyloidogenic proteins soluble during chemical mutagenesis, demonstrating it by mimicking phosphorylation and acetylation of amyloid-beta peptide.

bioRxiv · Jan 28, 2022Biochemistry

Small molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer's disease

G. T. Heller, F. A. Aprile, T. C. Michaels, R. Limbocker, M. Perni, F. S. Ruggeri, B. Mannini, T. Lohr, M. Bonomi, C. Camilloni, A. De Simone, I. C. Felli, R. Pierattelli, T. P. Knowles, C. M. Dobson, M. Vendruscolo

This paper identifies a small molecule that binds and sequesters monomeric amyloid-β, inhibiting its aggregation and rescuing toxicity in a C. elegans model.

bioRxiv · Sep 16, 2020Biophysics