Author

D. Mengin-Lecreulx

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

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 2 Research Focus:drug response / drug discovery· 2 Approach:experimental assay· 2 Assay:proteomics· 2 Organism:bacteria (other)· 1 Organism:chicken / avian· 1 Research Focus:differential expression· 1 Organism:mouse· 1

Frequent Co-Authors

B. Henrichfreise· 1 shared B. Tully· 1 shared B. Zellner· 1 shared C. Otten· 1 shared F. Corona· 1 shared G. Greub· 1 shared H. Buehl· 1 shared I. Loeckener· 1 shared

Activity by Year

2021-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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1 shared paperMicrobiology

B. Henrichfreise

Mutual co-authors in cluster

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2 papers

Recent·Most cited

An NlpC/P60 protein catalyzes a key step in peptidoglycan recycling at the intersection of energy recovery, cell division and immune evasion in the intracellular pathogen Chlamydia trachomatis

J. Reuter, C. Otten, N. Jacquier, J. Lee, D. Mengin-Lecreulx, I. Loeckener, R. Mayer, F. Corona, J. Dannenberg, S. Aeby, H. Buehl, G. Greub, W. Vollmer, T. Schneider, B. Henrichfreise

This study identifies an NlpC/P60 peptidase in Chlamydia trachomatis that recycles peptidoglycan to support cell division, energy recovery, and immune evasion.

bioRxiv · Nov 17, 2022Microbiology

A Francisella tularensis L,D-carboxypeptidase plays important roles in cell morphology, envelope integrity, and virulence.

B. Zellner, D. MENGIN-LECREULX, B. Tully, W. Gunning, R. Booth, J. F. Huntley

This study identifies an L,D-carboxypeptidase in F. tularensis essential for cell morphology, envelope integrity, and virulence.

bioRxiv · Jan 14, 2021Microbiology