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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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Sortase-Mediated Pilus Fiber Biogenesis in Streptococcus pneumoniae
Clothilde Manzano,Carlos Contreras-Martel,Lamya El Mortaji,Thierry Izoré,Daphna Fenel,Thierry Vernet,Guy Schoehn,Anne Marie Di Guilmi,Andréa Dessen +8 more
TL;DR: It is shown that SrtC-1 is the main pilus-polymerizing transpeptidase, and electron microscopy analyses of RrgB fibers reconstituted in vitro reveal they structurally mimic the pneumococcal pilus backbone.
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Mutations in the active site of penicillin-binding protein PBP2x from Streptococcus pneumoniae. Role in the specificity for β-lactam antibiotics
TL;DR: In vitro data presented here are in agreement with the distinct resistance profiles mediated by these mutations in vivo and underline their role as powerful resistance determinants.
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Crystal structure of penicillin-binding protein 1a (PBP1a) reveals a mutational hotspot implicated in beta-lactam resistance in Streptococcus pneumoniae.
Carlos Contreras-Martel,Viviana Job,Anne Marie Di Guilmi,Thierry Vernet,Otto Dideberg,Andréa Dessen +5 more
TL;DR: An analysis of P BP1a sequences from drug-resistant clinical strains in light of the structure reveals the existence of a mutational hotspot at the entrance of the catalytic cleft that leads to the modification of the polarity and accessibility of the mutated PBP1a active site.
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Structure-Based Phylogeny of the Metallo-β-Lactamases
TL;DR: The presence of genes from Eubacteria, Archaebacteria, and Eukaryota on that tree is consistent with a very ancient origin of the metallo-β-lactamase family.
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A multidimensional strategy to detect polypharmacological targets in the absence of structural and sequence homology.
Jacob D. Durrant,Rommie E. Amaro,Lei Xie,Michael D. Urbaniak,Michael A. J. Ferguson,Antti M. Haapalainen,Zhijun Chen,Anne Marie Di Guilmi,Frank Wunder,Philip E. Bourne,J. Andrew McCammon,J. Andrew McCammon +11 more
TL;DR: A multidimensional strategy for the identification of secondary targets of known small-molecule inhibitors in the absence of global structural and sequence homology with the primary target protein is introduced.