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Claire Durmort

Researcher at University of Grenoble

Publications -  30
Citations -  1136

Claire Durmort is an academic researcher from University of Grenoble. The author has contributed to research in topics: Peptidoglycan & Adherens junction. The author has an hindex of 16, co-authored 28 publications receiving 1005 citations. Previous affiliations of Claire Durmort include Joseph Fourier University & Centre national de la recherche scientifique.

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Journal ArticleDOI

Zinc uptake by Streptococcus pneumoniae depends on both AdcA and AdcAII and is essential for normal bacterial morphology and virulence.

Lucie Bayle, +8 more
- 01 Nov 2011 - 
TL;DR: The results show that AdcA and adcAII play an essential and redundant role in specifically importing zinc into the pneumococcus, and that both zinc transporters are required for proper cell division and for S. pneumoniae survival during infection.
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AdcAII, a new pneumococcal Zn-binding protein homologous with ABC transporters: biochemical and structural analysis.

Elodie Loisel, +7 more
- 05 Sep 2008 - 
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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The Interaction of Streptococcus pneumoniae with Plasmin Mediates Transmigration across Endothelial and Epithelial Monolayers by Intercellular Junction Cleavage

Cécile Attali, +3 more
- 01 Nov 2008 - 
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.
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On-chip microbial culture for the specific detection of very low levels of bacteria

Sihem Bouguelia, +10 more
- 18 Sep 2013 - 
TL;DR: In this paper, the authors combine concomitant "on-chip" microbial culture with sensitive surface plasmon resonance (SPR) detection of bacteria, thus allowing rapid specific detection of the bacteria pathogens.
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Structure of the fiber head of Ad3, a non-CAR-binding serotype of adenovirus.

Claire Durmort, +6 more
- 05 Jul 2001 - 
TL;DR: The receptor binding domain (head) of the Ad3 fiber protein has been expressed in Escherichia coli inclusion bodies and a strict conservation of the beta-sheet scaffold of the protein very similar to the head structures of the CAR-binding serotypes Ad2, Ad5, and Ad12.