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Alain Hehn

Researcher at University of Lorraine

Publications -  85
Citations -  3528

Alain Hehn is an academic researcher from University of Lorraine. The author has contributed to research in topics: Furanocoumarin & Phenylpropanoid. The author has an hindex of 30, co-authored 81 publications receiving 3077 citations. Previous affiliations of Alain Hehn include Centre national de la recherche scientifique & Institut national de la recherche agronomique.

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CYP98A3 from Arabidopsis thaliana Is a 3′-Hydroxylase of Phenolic Esters, a Missing Link in the Phenylpropanoid Pathway

TL;DR: It is shown that the gene encoding CYP98A3, which was the best possible P450 candidate for a 3-hydroxylase in the Arabidopsis genome, is highly expressed in inflorescence stems and wounded tissues and catalyzes the synthesis of chlorogenic acid and very likely also the 3-Hydroxylation of lignin monomers.
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Cytochromes P450 for engineering herbicide tolerance

TL;DR: The recovery of an increasing number of plant P450 genes in recombinant form has enabled their use in experimentation, which has revealed their extraordinary potential for engineering herbicide tolerance, biosafening, bioremediation and green chemistry.
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Biosynthesis of coumarins in plants: a major pathway still to be unravelled for cytochrome P450 enzymes

TL;DR: This review highlights the major steps of the coumarin pathway with emphasis on the cytochrome P450 enzymes involved, including Ortho-hydroxylation of hydroxycinnamic acids, and the outcomes of novel strategies developed to uncover cou marin-committed CYPs.
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Crosstalk and differential response to abiotic and biotic stressors reflected at the transcriptional level of effector genes from secondary metabolism.

TL;DR: Interestingly, a subset of genes induced by P. syringae was not responsive to the applied stress hormones, and homologous members within branches of these effector gene families displayed differential expression patterns either in both organs or during stress responses arguing for their non-redundant functions.
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Evolution of a novel phenolic pathway for pollen development.

TL;DR: A retroposition, neofunctionalization, and duplication sequence that, via selective and local amino acid replacement, led to the evolution of a novel phenolic pathway in Brassicaceae is described and shows how positive Darwinian selection can favor structured clusters of nonsynonymous substitutions that are needed for the transition of enzymes to new functions.