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Pierre Legrand

Researcher at Soleil Synchrotron

Publications -  140
Citations -  6683

Pierre Legrand is an academic researcher from Soleil Synchrotron. The author has contributed to research in topics: Infrared spectroscopy & Beamline. The author has an hindex of 39, co-authored 135 publications receiving 5845 citations. Previous affiliations of Pierre Legrand include French Institute of Health and Medical Research & Paul Sabatier University.

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Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center.

TL;DR: The structure of the heterodimeric Fe-only hydrogenase from Desulfovibrio desulfuricans is reported - the first for this class of enzymes and it is suggested that it was imported from the inorganic world as an already functional unit.
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Isolation and characterisation of mesenchymal stem cells from adult mouse bone marrow

TL;DR: Mouse MMSCs sharing the same morphological and functional characteristics as human MSCs can be successfully isolated from adult bone marrow without previous mouse or bone marrow treatment and it is demonstrated that this cell type after grafting in mouse pathology models has the MSC phenotype.
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Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase.

TL;DR: It is postulate that only the A-clusters containing two Ni ions are catalytically active in the tetrameric α2β2 acetyl-coenzyme A synthase/carbon monoxide dehydrogenase from Moorella thermoacetica.
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Crystal structure of the 14-subunit RNA polymerase I

TL;DR: The crystal structure of Pol I from Saccharomyces cerevisiae at 3.0 Å resolution shows a compact core with a wide DNA-binding cleft and a tightly anchored stalk, and an extended loop mimics the DNA backbone in the clefts and may be involved in regulating Pol I transcription.
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Structure and allosteric inhibition of excitatory amino acid transporter 1

TL;DR: The first crystal structures of a thermostabilized human SLC1 transporter, the excitatory amino acid transporter 1 (EAAT1), with and without allosteric and competitive inhibitors bound are presented, showing novel architectural features of the human transporters.