Author

G. Effantin

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· 4 Microbiology· 4 Biochemistry· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Assay:cryo-EM· 7 Research Focus:cell type annotation· 4 Approach:microscopy & imaging analysis· 4 Research Focus:protein structure prediction· 4 Assay:proteomics· 3 Approach:deep learning· 2 Organism:E. coli· 2

Frequent Co-Authors

G. Schoehn· 8 shared C. Breyton· 2 shared H. Wang· 2 shared R. Linares· 2 shared A. C. Sivertsen· 1 shared A. Desfosses· 1 shared A. Favier· 1 shared A. Lieber· 1 shared

Activity by Year

2018-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 13 mutual co-author links

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8 shared papersBiophysics

G. Schoehn

Mutual co-authors in cluster

Author profile →

10 papers

Recent·Most cited

Ultrastructural details of resistance factors of the bacterial spore revealed by in situ cryo-electron tomography

E. Bauda, B. Gallet, J. Moravcova, G. Effantin, H. Chan, J. Novacek, P.-H. Jouneau, C. D. A. Rodrigues, G. Schoehn, C. Moriscot, C. Morlot

This study uses cryo-electron tomography to reveal the ultrastructural organization of Bacillus subtilis spores, including the toroidal chromosome and nascent coat layers during sporulation.

bioRxiv · Jun 20, 2023 · PreprintMicrobiology

A natural single nucleotide mutation in the small regulatory RNA ArcZ of Dickeya solani switches off the antimicrobial activities against yeast and bacteria.

T. Brual, G. Effantin, J. Baltenneck, L. Attaiech, C. Grosbois, M. Royet, J. Cigna, D. Faure, N. Hugouvieux-Cotte-Pattat, E. Gueguen

The paper identifies a single-nucleotide mutation in the ArcZ sRNA gene of Dickeya solani that disables antimicrobial activities against yeast and bacteria.

PLOS Genetics · Apr 27, 2023Peer-reviewedMicrobiology

Deciphering bacteriophage T5 host recognition mechanism and infection trigger

S. Degroux, G. Effantin, R. Linares, G. Schoehn, C. Breyton

This study determines the structure of bacteriophage T5 RBPpb5 bound to its E. coli receptor FhuA, revealing the mechanism of host recognition and infection initiation.

bioRxiv · Sep 22, 2022Biophysics

Structural basis of bacteriophage T5 infection trigger and E. coli cell wall perforation

R. Linares, C.-A. Arnaud, G. Effantin, C. Darnault, N. H. Epalle, E. Boeri Erba, G. Schoehn, C. Breyton

This paper presents the structure of bacteriophage T5 tip and its interaction with E. coli receptor FhuA, revealing conformational changes during infection and cell wall perforation.

bioRxiv · Sep 20, 2022Microbiology

Three-dimensional envelope and subunit interactions of the plastid-encoded RNA polymerase from Sinapis alba

R. Ruedas, Y. Coute, S. Kieffer-Jaquinod, S. Sankari Muthukumar, F.-X. Gillet, D. Fenel, G. Effantin, T. Pfannschmidt, R. Blanvillain, D. Cobessi

This study determines the 3D structure of the plastid-encoded RNA polymerase (PEP) from Sinapis alba and identifies subunit interactions through proteomics and electron microscopy.

bioRxiv · May 4, 2022Biochemistry

Structural basis of CHMP2A-CHMP3 ESCRT-III polymer assembly and membrane cleavage

K. Azad, D. Guilligay, C. Boscheron, S. Maity, N. De Franceschi, G. Sulbaran, G. Effantin, H. Wang, J.-P. Kleman, P. Bassereau, G. Schoehn, W. Roos, A. Desfosses, W. Weissenhorn

This study presents cryo-EM structures of CHMP2A-CHMP3 ESCRT-III filaments and shows they constrict and cleave membrane tubes through electrostatic interactions and VPS4-mediated remodeling.

bioRxiv · Apr 12, 2022Cell Biology

Reversible supramolecular assembly of the anti-microbial peptide plectasin into helical non-amyloid fibrils

C. Pohl, G. Effantin, E. Kandiah, S. Meier, G. Zeng, W. Streicher, G. H. Peters, G. Schoehn, C. Mueller-Dieckmann, A. Noergaard, P. Harris

The paper shows that a triple-mutant of plectasin forms reversible helical non-amyloid fibrils, with high-resolution structure and pH-dependent equilibrium.

bioRxiv · Sep 6, 2021 · PreprintBiophysics

Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes

B. Arragain, G. Effantin, P. Gerlach, J. Reguera, G. Schoehn, S. Cusack, H. Malet

This study presents the cryo-EM structures of La Crosse virus polymerase in pre-initiation and elongation states, revealing conformational changes important for transcription.

Nature Communications · Jul 17, 2020Peer-reviewedBiophysics

Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex

D. Gauto, L. Estrozi, C. Schwieters, G. Effantin, P. Macek, r. sounier, A. C. Sivertsen, E. Schmidt, R. Kerfah, G. Mas, J.-P. Colletier, P. Guntert, A. Favier, G. Schoehn, J. Boisbouvier, P. Schanda

The paper integrates NMR and cryo-EM to determine the atomic structure of a large enzyme complex, achieving high precision and accuracy beyond the limitations of each method individually.

bioRxiv · Dec 16, 2018Biophysics

Cryo-EM structure of adenovirus type 3 fibre with desmoglein 2 shows a novel mode of receptor engagement

E. Vassal-Stermann, G. Effantin, C. Zubieta, W. P. Burmeister, F. Iseni, H. Wang, A. Lieber, G. Schoehn, P. Fender

The paper determines the cryo-EM structure of a complex between adenovirus type 3 fibre knob and desmoglein 2, revealing a novel receptor engagement mechanism.

bioRxiv · Nov 16, 2018Microbiology