Author

J. Schymkowitz

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 Cancer Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 3 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Organism:E. coli· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

F. Rousseau· 4 shared M. Ramakers· 3 shared C. Morelli· 2 shared D. Audenaert· 2 shared E. Michiels· 2 shared S. D'Haeyer· 2 shared T. Garcia· 2 shared V. Goossens· 2 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

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4 shared papersBiophysics

F. Rousseau

Mutual co-authors in cluster

Author profile →

4 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

The dynamic transition of persistence towards the VBNC state during stationary phase is driven by protein aggregation

L. Dewachter, C. Bollen, D. Wilmaerts, E. Louwagie, P. Herpels, P. Matthay, L. Khodaparast, L. Khodaparast, F. Rousseau, J. Schymkowitz, J. Michiels

This study shows that bacterial persistence during stationary phase is linked to protein aggregation and ATP depletion, with ObgE playing a role in triggering this process.

bioRxiv · Feb 15, 2021Microbiology

The tumor suppressor protein PTEN undergoes amyloid-like aggregation in tumor cells.

F. Claes, E. Maritschnegg, G. De Baets, A. Siekierska, M. Saiz Rubio, M. Ramakers, E. Michiels, F. De Smet, J. Depreeuw, I. Vergote, A. Vanderstichele, A. van den Broeck, S. Olbrecht, E. Hermans, F. Amant, , J. Schymkowitz

This study shows PTEN, a tumor suppressor, undergoes amyloid-like aggregation in tumor cells, both due to mutations and dysregulated protein homeostasis, and links this aggregation to poor clinical outcomes.

bioRxiv · Nov 30, 2020 · PreprintCancer Biology