Author

A. Lamy

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· 3 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell type annotation· 3 Research Focus:host-pathogen & immune response· 2 Organism:mouse· 2 Research Focus:chromatin & epigenetic regulation· 1 Assay:DNA methylation· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

R. P.-A. Berntsson· 2 shared W.-S. Sun· 2 shared A. Breidenstein· 1 shared A. Peralvarez-Marin· 1 shared C. P. J. Bader· 1 shared E. Macarini-Bruzaferro· 1 shared F. Bringaud· 1 shared F. Jaeger· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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2 shared papersBiochemistry

R. P.-A. Berntsson

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

PrgE: an OB-fold protein from plasmid pCF10 with striking differences to prototypical bacterial SSBs

A. Breidenstein, A. Lamy, C. P. J. Bader, W.-S. Sun, P. H. Wanrooij, R. P.-A. Berntsson

The paper characterizes PrgE, a non-essential SSB from plasmid pCF10, showing it binds both single- and double-stranded DNA with unique quaternary assembly and DNA-binding properties.

bioRxiv · Mar 13, 2024 · PreprintBiochemistry

A novel lipase with dual localisation in Trypanosoma brucei

S. Monic, A. Lamy, T. Magali, T. Bizarra-Rebelo, F. Bringaud, T. K. Smith, L. M. Figueiredo, L. Riviere

The paper identifies a novel lipase in Trypanosoma brucei with dual localization and excretion, suggesting its potential as a diagnostic tool.

bioRxiv · Feb 23, 2022Microbiology

Structure of the enterococcal T4SS protein PrgL reveals unique dimerization interface in the VirB8 protein family

F. Jaeger, A. Lamy, N. Guerini, W.-S. Sun, R. P.-A. Berntsson

The paper determines the structure of the enterococcal T4SS protein PrgL, revealing a unique dimerization interface compared to other VirB8-like proteins.

bioRxiv · Oct 30, 2020Biochemistry

ATP2, the essential P4-ATPase of malaria parasites, catalyzes lipid-dependent ATP hydrolysis in complex with a Cdc50 β-subunit

A. Lamy, E. Macarini-Bruzaferro, A. Peralvarez-Marin, M. le Maire, J. L. Vazquez-Ibar

This study investigates the function and structural organization of the malaria parasite ATP2, showing it forms a complex with Cdc50 proteins and catalyzes ATP hydrolysis in the presence of specific phospholipids.

bioRxiv · Jun 8, 2020Biochemistry