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Eric Le Cam

Researcher at Université Paris-Saclay

Publications -  96
Citations -  4667

Eric Le Cam is an academic researcher from Université Paris-Saclay. The author has contributed to research in topics: DNA & DNA repair. The author has an hindex of 34, co-authored 87 publications receiving 4209 citations. Previous affiliations of Eric Le Cam include Institut Gustave Roussy & University of Paris-Sud.

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The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments.

TL;DR: It is shown that DNA strand exchange mediated in vitro by Rad51 is inhibited by Srs2, and that SRS2 disrupts Rad51 filaments formed on single-stranded DNA, providing an explanation for the anti-recombinogenic role of Srs1 in vivo and highlighting a previously unknown mechanism for recombination control.
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UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli

TL;DR: It is shown that UvrD, but not Rep, directly prevents homologous recombination in vivo, and evidence that RecA contributes to toxicity in the rep uvrD mutant is provided.
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Hypoxic tumor-derived microvesicles negatively regulate NK cell function by a mechanism involving TGF-β and miR23a transfer.

TL;DR: This is the first study to show that hypoxic tumor cells by secreting MVs can educate NK cells and decrease their antitumor immune response, and highlights the existence of a novel mechanism of immune suppression mediated by hypoxic TD-MVs.
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A Key Presynaptic Role in Transformation for a Widespread Bacterial Protein: DprA Conveys Incoming ssDNA to RecA

TL;DR: It is proposed that DprA is a new member of the recombination-mediator protein family, dedicated to natural bacterial transformation, and it is shown that while the Escherichia coli ssDNA-binding protein SSB limits access of RecA to ssDNA, DPRA lowers this barrier.
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Adsorption of DNA to mica mediated by divalent counterions: a theoretical and experimental study.

TL;DR: A model suggests that DNA attraction is due to the sharing of the DNA and mica counterions, and it is explained how a reversible binding of theDNA molecules can be obtained with a pretreated mica surface.