Author

M. Rolando

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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Microbiology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:host-pathogen & immune response· 2 Organism:bacteria (other)· 1 Assay:ChIP-seq· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:development & morphogenesis· 1 Organism:human· 1

Frequent Co-Authors

C. Buchrieser· 3 shared A. Blanco· 1 shared A. Louche· 1 shared A. M. Wehenkel· 1 shared C. Berge· 1 shared C. Di Silvestre· 1 shared C. Lionnet· 1 shared C. Rusniok· 1 shared

Activity by Year

2018-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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3 shared papersMicrobiology

C. Buchrieser

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Legionella para-effectors target chromatin and promote bacterial replication

D. Schator, S. Mondino, J. Berthelet, C. Di Silvestre, M. Ben Asssya, C. Rusniok, F. Rodreigues-Lima, A. M. Wehenkel, C. Buchrieser, M. Rolando

This study identifies two Legionella effectors, LphD and RomA, that work together to modify host chromatin and promote bacterial replication.

bioRxiv · Oct 16, 2022 · PreprintMicrobiology

The unique Brucella effectors NyxA and NyxB target SENP3 to modulate the subcellular localisation of nucleolar proteins

A. Louche, A. Blanco, T. L. Lacerda, C. Lionnet, C. Berge, M. Rolando, F. Lembo, J.-P. Borg, C. Buchrieser, M. Nagahama, J.-P. Gorvel, V. Gueguen-Chaignon, L. Terradot, S. P. Salcedo

This study shows that Brucella effectors NyxA and NyxB target SENP3 to alter nucleolar protein localization, promoting bacterial replication.

bioRxiv · Apr 23, 2021 · PreprintMicrobiology

A Ca2+-regulated deAMPylation switch in bacterial and human FIC proteins.

S. Veyron, G. Oliva, M. Rolando, C. Buchrieser, G. Peyroche, J. Cherfils

This study identifies Ca2+ as a diffusible signal that modulates AMPylation and deAMPylation activities in FIC proteins by controlling a conserved glutamate's role in metal-dependent enzyme function.

bioRxiv · Aug 3, 2018Biochemistry