Author

C. Galvagnion

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· 1 Bioengineering· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 3 Research Focus:cell type annotation· 2 Research Focus:host-pathogen & immune response· 2 Assay:proteomics· 2 Research Focus:differential expression· 1 Organism:Drosophila· 1 Assay:metabolomics· 1

Frequent Co-Authors

A. H. V. Schapira· 1 shared A. K. Buell· 1 shared A. Nagpal· 1 shared A. Voigt· 1 shared B. H. Falkenburger· 1 shared C. M. Dobson· 1 shared D. A. Di Monte· 1 shared D. Komnig· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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1 shared paperBiochemistry

A. H. V. Schapira

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Author profile →

3 papers

Recent·Most cited

Lipid levels correlate with neuronal and dopaminergic markers during the differentiation of SH-SY5Y cells

F. R. Marlet, S. S. Munoz, N. Sotiraki, J. N. Eliasen, J. P. Woessmann, J. E. Dreier, E. M. Schoof, K. A. Kohlmeier, K. Maeda, C. Galvagnion

This study characterizes lipidome changes during SH-SY5Y cell differentiation into dopaminergic neurons and links lipid levels to neuronal and dopaminergic markers.

bioRxiv · Sep 1, 2023Cell Biology

Sphingolipid changes in Parkinson L444P GBA mutation fibroblasts promote α-synuclein aggregation

C. Galvagnion, S. Cerri, A. H. V. Schapira, F. Blandini, D. A. Di Monte

This study shows that the L444P GBA mutation in fibroblasts alters sphingolipid profiles, promoting α-synuclein aggregation through lipid-induced fibrillation.

bioRxiv · Nov 9, 2020Biochemistry

An engineered monomer binding-protein for α-synucleinefficiently inhibits the proliferation of amyloid fibrils

E. D. Agerschou, T. Saridaki, P. Flagmeier, C. Galvagnion, D. Komnig, A. Nagpal, N. Gasterich, L. Heid, V. Prasad, H. Shaykhalishahi, A. Voigt, D. Willbold, C. M. Dobson, B. H. Falkenburger, W. Hoyer, A. K. Buell

The paper engineers a monomer-binding protein that inhibits α-synuclein fibril proliferation in vitro and in vivo, showing it reduces aggregates and related pathologies.

bioRxiv · Mar 5, 2019Bioengineering