Author

F. Raimondi

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 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Organism:Drosophila· 1 Assay:protein structure· 1

Frequent Co-Authors

C. J. Gloeckner· 2 shared G. Guaitoli· 2 shared A. Cezanne· 1 shared A. Kortholt· 1 shared A. N. Lupas· 1 shared D. Fessas· 1 shared D. St Johnston· 1 shared E. Los· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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2 shared papersBiochemistry

C. J. Gloeckner

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Author profile →

3 papers

Recent·Most cited

Biophysical analysis reveals autophosphorylation as an important negative regulator of LRRK2 dimerization

G. Guaitoli, X. Zhang, F. Saitta, P. Miglionico, L. M. Silbermann, F. Y. Ho, F. von Zweydorf, M. Signorelli, K. Tych, D. Fessas, F. Raimondi, A. Kortholt, C. J. Gloeckner

This study uses biophysical methods to show that autophosphorylation inhibits LRRK2 dimerization, suggesting it as a negative regulator with implications for Parkinson's disease.

bioRxiv · Aug 11, 2023 · PreprintBiochemistry

RhoGAP19D inhibits Cdc42 laterally to control epithelial cell shape and prevent invasion

W. Fic, R. Bastock, F. Raimondi, E. Los, Y. Inoue, J. Gallop, R. B. Russell, D. St Johnston

The paper identifies RhoGAP19D as a Cdc42 GTPase Activating Protein that restricts Cdc42 activity to the apical domain, preventing epithelial invasion.

bioRxiv · Sep 17, 2020Cell Biology

Allosteric structural alterations and auto-regulation of Rab5 GEF activity in Rabex5

J. Lauer, A. Cezanne, G. Guaitoli, F. Raimondi, M. Gentzel, V. Alva, M. Habeck, M. Ueffing, A. N. Lupas, C. J. Gloeckner, M. Zerial

This study reevaluates the autoinhibition mechanism of Rabex5 by analyzing structural changes and nucleotide exchange activity, revealing new regulatory roles for Ubiquitin binding domains.

bioRxiv · Feb 27, 2019 · PreprintBiophysics