Author

V. Goossens

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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Biophysics· 2

Signature Assays, Organisms & Methods

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Organism:human· 2 Assay:cryo-EM· 1 Approach:experimental assay· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Assay:protein sequence· 1 Approach:statistical model· 1

Frequent Co-Authors

C. Morelli· 2 shared D. Audenaert· 2 shared F. Rousseau· 2 shared J. Schymkowitz· 2 shared M. Ramakers· 2 shared S. D'Haeyer· 2 shared T. Garcia· 2 shared D. R. Thal· 1 shared

Activity by Year

2021-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 43 mutual co-author links

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2 shared papersBiophysics

C. Morelli

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2 papers

Recent·Most cited

Tau amyloid polymorphism is shaped by local structural propensities of its protein sequence

N. Louros, M. Wilkinson, G. Tsaka, M. Ramakers, C. Morelli, T. Garcia, R. U. Gallardo, S. D'Haeyer, V. Goossens, D. Audenaert, D. R. Thal, N. A. Ranson, S. E. Radford, F. Rousseau, J. Schymkowitz

The paper identifies a C-terminal tau peptide that adopts polymorphic conformations contributing to disease-specific tau filament folds and propagation.

bioRxiv · Oct 24, 2022 · PreprintBiophysics

Mapping the sequence specificity of heterotypic amyloid interactions enables the identification of aggregation modifiers

N. N. Louros, M. Ramakers, E. Michiels, K. Konstantoulea, C. Morelli, T. Garcia, S. D'Haeyer, V. Goossens, D. Audenaert, F. Rousseau, J. Schymkowitz

The paper identifies sequence-specific rules governing heterotypic amyloid interactions and shows how they can modify amyloid assembly and contribute to neurodegenerative disease progression.

bioRxiv · Jun 4, 2021Biophysics