Author

A. Possenti

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 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:deep learning· 2 Research Focus:drug response / drug discovery· 2 Research Focus:cell type annotation· 1 Approach:experimental assay· 1 Organism:human· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

M. Nowinska· 2 shared M. Vendruscolo· 2 shared R. I. Horne· 2 shared R. Staats· 2 shared S. Chia· 2 shared T. P. J. Knowles· 2 shared Z. F. Brotzakis· 2 shared A. Aubert· 1 shared

Activity by Year

2021-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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2 shared papersBiophysics

M. Nowinska

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Structure-based discovery of small molecule inhibitors of the autocatalytic proliferation of alpha-synuclein aggregates

S. Chia, Z. F. Brotzakis, R. I. Horne, A. Possenti, B. Mannini, R. Cataldi, M. Nowinska, R. Staats, S. Linse, T. P. J. Knowles, J. Habchi, M. Vendruscolo

This study identifies small molecules that inhibit alpha-synuclein aggregate proliferation using structure-based and kinetic assays.

Molecular Pharmaceutics · Nov 14, 2022Peer-reviewedBiophysics

Functional characterization of the thrombospondin-related paralogous proteins rhoptry discharge factor 1 and 2 unveils phenotypic plasticity in Toxoplasma gondii rhoptry exocytosis

A. Possenti, M. Di Cristina, C. Nicastro, M. Lunghi, V. Messina, F. Piro, L. Tramontana, S. Cherchi, M. Falchi, L. Bertuccini, F. Spano

This study identifies and characterizes RDF1 and RDF2, two T. gondii proteins essential for rhoptry exocytosis, revealing a compensatory mechanism that contributes to phenotypic plasticity.

bioRxiv · Mar 2, 2022Microbiology

Discovery of Potent Inhibitors of α-Synuclein Aggregation Using Structure-Based Iterative Learning

R. I. Horne, E. Andrzejewska, P. Alam, Z. F. Brotzakis, A. Srivastava, A. Aubert, M. Nowinska, R. C. Gregory, R. Staats, A. Possenti, S. Chia, P. Sormanni, B. Ghetti, B. Caughey, T. P. J. Knowles, M. Vendruscolo

This paper uses structure-based machine learning to identify potent small molecule inhibitors of α-synuclein aggregation, achieving compounds two orders of magnitude more potent than previous reports.

bioRxiv · Nov 10, 2021Biophysics