Author

A. Cezanne

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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Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Research Focus:development & morphogenesis· 1 Assay:imaging· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Approach:statistical model· 1

Frequent Co-Authors

J. Lauer· 2 shared M. Zerial· 2 shared A. Arashiro Pulschen· 1 shared A. N. Lupas· 1 shared A. Saric· 1 shared A. Solomatina· 1 shared B. Baum· 1 shared C. J. Gloeckner· 1 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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2 shared papersBiochemistry

J. Lauer

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

The patterned assembly and stepwise Vps4-mediated disassembly of composite ESCRT-III polymers drives archaeal cell division

F. Hurtig, T. C. Q. Burgers, A. Cezanne, X. Jiang, F. N. Mol, J. Traparic, G. Tarrason Risa, A. Arashiro Pulschen, L. Harker-Kirschneck, A. Saric, R. Vlijm, B. Baum

The paper uses super-resolution microscopy and computational modeling to show how CdvB/CdvB1/CdvB2 proteins form a patterned composite ESCRT-III division ring that disassembles stepwise to drive archaeal cell division.

bioRxiv · Sep 16, 2022Cell Biology

A non-linear system patterns Rab5 GTPase on the membrane

A. Cezanne, J. Lauer, A. Solomatina, I. F. Sbalzarini, M. Zerial

The paper demonstrates that Rab5 GTPase forms membrane patterns through a handover mechanism involving Rabex5/Rabaptin5 and requires an endosomal lipid composition.

bioRxiv · Dec 17, 2019Biochemistry

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