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Anne Marie Di Guilmi
Researcher at University of Grenoble
Publications - 44
Citations - 2116
Anne Marie Di Guilmi is an academic researcher from University of Grenoble. The author has contributed to research in topics: Peptidoglycan & Penicillin binding proteins. The author has an hindex of 28, co-authored 41 publications receiving 1980 citations. Previous affiliations of Anne Marie Di Guilmi include French Alternative Energies and Atomic Energy Commission & Joseph Fourier University.
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Oligomerization of type III secretion proteins PopB and PopD precedes pore formation in Pseudomonas.
Guy Schoehn,Anne Marie Di Guilmi,David Lemaire,Ina Attree,Winfried Weissenhorn,Andréa Dessen +5 more
TL;DR: Formation of metastable oligomers precedes membrane association and ring generation in the formation of the Pseudomonas translocon, a mechanism which may be similar for other pathogens that employ type III secretion systems.
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Structural Basis of Host Cell Recognition by the Pilus Adhesin from Streptococcus pneumoniae
Thierry Izoré,Carlos Contreras-Martel,Lamya El Mortaji,Clothilde Manzano,Rémy Terrasse,Thierry Vernet,Anne Marie Di Guilmi,Andréa Dessen +7 more
TL;DR: It is shown by site-specific mutagenesis, mass spectrometry, and thermal shift assays that intradomain isopeptide bonds play key roles in stabilizing RrgA's stalk, which suggests common strategies for ECM recognition and immune evasion.
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AdcAII, a new pneumococcal Zn-binding protein homologous with ABC transporters: biochemical and structural analysis.
Elodie Loisel,Lilian Jacquamet,Laurence Serre,Cédric Bauvois,Jean Luc Ferrer,Thierry Vernet,Anne Marie Di Guilmi,Claire Durmort +7 more
TL;DR: Functional and structural data provide new perspectives related to the physiological role of AdcAII in pneumococcus Zn homeostasis and a phylogenetic tree built from the sequence alignment of 68 proteins reveals a subgroup of members displaying an unusual genetic operon organisation.
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Active site restructuring regulates ligand recognition in class A penicillin-binding proteins
Pauline Macheboeuf,Anne Marie Di Guilmi,Viviana Job,Thierry Vernet,Otto Dideberg,Andréa Dessen +5 more
TL;DR: The structure of PBP1b* complexed with beta-lactam antibiotics reveals that ligand recognition requires a conformational modification involving conserved elements within the cleft, and suggest how class A PBPs may become activated as novel peptidoglycan synthesis becomes necessary during the cell division process.
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The Interaction of Streptococcus pneumoniae with Plasmin Mediates Transmigration across Endothelial and Epithelial Monolayers by Intercellular Junction Cleavage
TL;DR: The results highlight a novel function for the plasminogen recruitment at the bacterial surface in facilitating adherence of pneumococci to endothelial and epithelial cells, while active plAsmin degrades intercellular junctions.