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Chantal Hellal-Levy

Researcher at French Institute of Health and Medical Research

Publications -  7
Citations -  521

Chantal Hellal-Levy is an academic researcher from French Institute of Health and Medical Research. The author has contributed to research in topics: Mineralocorticoid receptor & Receptor. The author has an hindex of 6, co-authored 7 publications receiving 503 citations.

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Antagonism in the human mineralocorticoid receptor

TL;DR: A new mechanism of antagonism is proposed in which the AF2‐AD core region is destabilized by the loss of contacts between the antagonist and the helix H12 region, proposed in the light of the hMR homology model.
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Specific hydroxylations determine selective corticosteroid recognition by human glucocorticoid and mineralocorticoid receptors.

TL;DR: The ability of corticosteroids to stimulate the receptor's transactivation function is depending on the stability of the steroid‐receptor complexes, and it is proposed that contacts through the C21 hydroxyl group are sufficient to stabilize hMR but not hGR.
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Mechanistic aspects of mineralocorticoid receptor activation.

TL;DR: The key residues involved in the recognition of agonist and antagonist ligands are described and a two-step model with a dynamic dimension for the MR activation is proposed that is less efficient than aldosterone in stimulating the hMR transactivation.
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Crucial Role of the H11-H12 Loop in Stabilizing the Active Conformation of the Human Mineralocorticoid Receptor

TL;DR: It is proposed that the integrity of the H11-H12 loop is crucial for folding the receptor into a ligand-binding competent state and for establishing the network of contacts that stabilize the active receptor conformation.
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Folding Requirements of the Ligand-Binding Domain of the Human Mineralocorticoid Receptor

TL;DR: The results support the idea that a short sequence upstream of the LBD is essential for the interaction of hMR with hsp90 and that the C terminus of h MR and hSp90 are both essential for folding of the receptor in a high-affinity hormone-binding state.