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Pascal Dollé

Researcher at French Institute of Health and Medical Research

Publications -  169
Citations -  26799

Pascal Dollé is an academic researcher from French Institute of Health and Medical Research. The author has contributed to research in topics: Retinoic acid & Retinoic acid receptor. The author has an hindex of 82, co-authored 167 publications receiving 25579 citations. Previous affiliations of Pascal Dollé include University of Strasbourg & Paris Descartes University.

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Gene dosage-dependent effects of the Hoxa-13 and Hoxd-13 mutations on morphogenesis of the terminal parts of the digestive and urogenital tracts

TL;DR: Hoxa-13 and Hoxd-13 play important roles in the morphogenesis of the terminal part of the gut and urogenital tract during embryogenesis and postnatal development, demonstrating that both genes act, in a partly redundant manner, during early Morphogenesis of posterior trunk structures.
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Inactivation of the Friedreich ataxia mouse gene leads to early embryonic lethality without iron accumulation

TL;DR: It is suggested that the milder phenotype in humans is due to residual frataxin expression associated with the expansion mutations, and no iron accumulation was observed during embryonic resorption, suggesting that cell death could be due to a mechanism independent of iron accumulation.
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In vivo functional analysis of the Hoxa-1 3′ retinoic acid response element (3′RARE)

TL;DR: It is found that this enhancer plays an important role in the early establishment of the Hoxa-1 anterior expression boundary in the neural plate, providing strong evidence for direct control of Hox gene function by retinoids during normal development.
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Specific spatial and temporal distribution of retinoic acid receptor gamma transcripts during mouse embryogenesis.

TL;DR: It is suggested that RAR-gamma plays a crucial role for transducing RA signals at the level of gene expression during morphogenesis, chondrogenesis and differentiation of squamous epithelia.
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Characterization of a premeiotic germ cell-specific cytoplasmic protein encoded by Stra8, a novel retinoic acid-responsive gene.

TL;DR: Two- dimensional gel analysis and dephosphorylation experiments revealed that the two stereoisomers of RA differentially regulate the phosphorylation status of the Stra8 protein, which was shown to exist in differently phosphorylated forms.