Author

V. De Filippis

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· 3

Signature Assays, Organisms & Methods

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

Frequent Co-Authors

F. Uliana· 2 shared L. Acquasaliente· 2 shared A. Fossati· 1 shared A. Negro· 1 shared A. Pagotto· 1 shared C. M. Radu· 1 shared D. Peterle· 1 shared E. Ruben· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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2 shared papersBiochemistry

F. Uliana

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Author profile →

3 papers

Recent·Most cited

Human -Synuclein Inhibits Platelets Aggregation in vitro by Interfering with the -Thrombin/Protease-Activated Receptor 1 Functional Axis

G. Pontarollo, L. Acquasaliente, C. M. Radu, D. Peterle, I. Artusi, A. Pagotto, F. Uliana, P. Simioni, A. Negro, V. De Filippis

This study shows that human -synuclein inhibits platelet aggregation by interfering with the -thrombin/PAR1 functional axis through direct and indirect mechanisms.

bioRxiv · Mar 28, 2021 · PreprintBiochemistry

Mapping specificity, entropy, allosteric changes and substrates in blood proteases by a high-throughput protease screen

F. Uliana, M. Vizovisek, L. Acquasaliente, R. Ciuffa, A. Fossati, F. Frommelt, M. Gstaiger, V. De Filippis, U. auf dem Keller, R. Aebersold

The paper introduces a high-throughput proteomic method to profile protease activity and substrate specificity in native conditions, achieving high throughput and accuracy.

bioRxiv · Jul 20, 2020Biochemistry

X-ray and solution structures of human beta-2 glycoprotein I reveal a new mechanism of autoantibody recognition

E. Ruben, W. Planer, M. Chinnaraj, Z. Chen, X. Zuo, V. Pengo, V. De Filippis, R. Alluri, K. McCrae, P. Macor, F. Tedesco, N. Pozzi

This paper reveals the structure of human beta-2 glycoprotein I and shows that its elongated, flexible conformation allows autoantibodies to recognize an epitope without phospholipids.

bioRxiv · Feb 25, 2020Biochemistry