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Eric Dausse

Researcher at University of Bordeaux

Publications -  60
Citations -  1481

Eric Dausse is an academic researcher from University of Bordeaux. The author has contributed to research in topics: Aptamer & Systematic evolution of ligands by exponential enrichment. The author has an hindex of 21, co-authored 60 publications receiving 1419 citations. Previous affiliations of Eric Dausse include European Institute & French Institute of Health and Medical Research.

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Mapping of a novel gene for familial hypertrophic cardiomyopathy to chromosome 11.

TL;DR: The data suggest the localization of the novel FHC gene in a region spanning 17 centiMorgans, with significant linkage of the disease locus to several (CA)n repeats located on chromosome 11.
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DNA Aptamers Selected Against the HIV-1trans-Activation-responsive RNA Element Form RNA-DNA Kissing Complexes

TL;DR: In vitro selection was performed in a DNA library, made of oligonucleotides with a 30-nucleotide random sequence, to identify ligands of the human immunodeficiency virus type-1 trans-activation-responsive (TAR) RNA element, allowing the identification of a new type of complex, DNA-RNA kissing complex.
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Familial hypertrophic cardiomyopathy. Microsatellite haplotyping and identification of a hot spot for mutations in the beta-myosin heavy chain gene.

TL;DR: Haplotyping of polymorphic markers in close linkage to the beta-myosin heavy chain gene can provide rapid analysis of non informative pedigrees and rapid detection of carrier status, and indicate that codon 403 of the Beta- myosinheavy chain gene is a hot spot for mutations causing FHC.
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Diagnostic performance of QT interval variables from 24-h electrocardiography in the long QT syndrome

TL;DR: QT interval variables obtained from 24-h ECG recordings improve long QT syndrome diagnosis by showing an increased nocturnal ventricular repolarization rate-dependence in genotyped chromosome 11-linked patients.
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Selective inhibitory DNA aptamers of the human RNase H1

TL;DR: Using SELEX, a set of DNA sequences that can bind efficiently (K(d) values ranging from 10 to 80 nM) to the human RNase H1 are generated, confirming that double-stranded DNA does not constitute a trivial ligand for the enzyme.