Author

D. M. Vadukul

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1 Research Focus:host-pathogen & immune response· 1 Assay:protein structure· 1

Frequent Co-Authors

F. A. Aprile· 3 shared R. J. Thrush· 2 shared A. Huyghebaert· 1 shared C. Vrancx· 1 shared D. Tanase· 1 shared F. Raguseo· 1 shared J. Li· 1 shared J. Wang· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersBiochemistry

F. A. Aprile

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Author profile →

4 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

Cell-derived hexameric β-amyloid: a novel insight into composition, self-assembly and nucleating properties

D. M. Vadukul, C. Vrancx, P. Burguet, S. Contino, N. Suelves, L. C. Serpell, L. Quinton, P. Kienlen-Campard

This study identifies and characterizes cell-derived hexameric Aβ42, showing its nucleating properties and dependence on monomer availability in amyloid self-assembly.

bioRxiv · Dec 15, 2020 · PreprintBiochemistry