Author

L. Ballut

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· 2 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell type annotation· 2 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1 Research Focus:host-pathogen & immune response· 1 Organism:plant (other)· 1

Frequent Co-Authors

A. E. Miele· 1 shared C. Guillon· 1 shared C. Louvat· 1 shared C. Rocchi· 1 shared D. Lener· 1 shared F. Delolme· 1 shared F. Fiorini· 1 shared F. Ruaudel· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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1 shared paperBiochemistry

A. E. Miele

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3 papers

Recent·Most cited

The HIV-1 Integrase C-Terminal domain induces TAR RNA structural changes promoting Tat binding.

C. Rocchi, C. Louvat, A. E. Miele, J. Batisse, C. Guillon, L. Ballut, D. Lener, M. Negroni, M. Ruff, P. Gouet, F. Fiorini

This study shows that the HIV-1 Integrase C-terminal domain interacts with TAR RNA, inducing structural changes that facilitate Tat binding and displace IN from TAR.

bioRxiv · Oct 21, 2021Biochemistry

Scaffolding protein GspB/OutB facilitates assembly of the Dickeya dadantii type 2 secretion system by anchoring the outer membrane secretin pore to the inner membrane and to the peptidoglycan cell wall.

S. Zhang, S. Gu, P. Rycroft, F. Ruaudel, F. Delolme, X. Robert, L. Ballut, R. W. Pickersgill, V. E. Shevchik

This paper shows that GspB scaffolds the T2SS secretin pore in Dickeya dadantii by anchoring it to the inner membrane and peptidoglycan, and identifies its conserved periplasmic domain and interactions with GspD.

bioRxiv · Aug 6, 2021Microbiology

Helices on interdomain interface couple catalysis in the ATPPase domain with allostery in Plasmodium falciparum GMP synthetase

S. Shivakumaraswamy, N. Pandey, L. Ballut, S. Violot, N. Aghajari, H. Balaram

This study identifies helices at the interdomain interface of Plasmodium falciparum GMP synthetase that couple ATPPase catalysis with GATase activation through domain crosstalk.

bioRxiv · Feb 11, 2020Biochemistry