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Dominique Madern

Researcher at University of Grenoble

Publications -  55
Citations -  2677

Dominique Madern is an academic researcher from University of Grenoble. The author has contributed to research in topics: Malate dehydrogenase & Allosteric regulation. The author has an hindex of 28, co-authored 53 publications receiving 2457 citations. Previous affiliations of Dominique Madern include French Alternative Energies and Atomic Energy Commission & Commissariat à l'énergie atomique et aux énergies alternatives.

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Halophilic adaptation of enzymes.

TL;DR: It is described how thermodynamic observations, such as parameters pertaining to solvent–protein interactions or enzyme-unfolding kinetics, depend strongly on solvent composition and reveal the important role played by water and ion binding to halophilic proteins.
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Adaptation to extreme environments: macromolecular dynamics in bacteria compared in vivo by neutron scattering.

TL;DR: Effective force constants determining the mean macromolecular resilience were found to increase with physiological temperature, indicating that the increase in stabilization free energy is dominated by enthalpic rather than entropic terms.
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Molecular evolution within the L-malate and L-lactate dehydrogenase super-family.

TL;DR: A refined evolutionary scenario of the NAD(P)-dependent malate and NAD-dependent lactate super-family is elaboration, in which the selection of L-LDH and the fate of L -MalDH during mitochrondrial genesis are presented.
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Phylogenetically driven sequencing of extremely halophilic archaea reveals strategies for static and dynamic osmo-response.

TL;DR: A generalized model for haloarchaeal management of cytoplasmic osmolarity in response to osmotic shifts is proposed, where potassium accumulation and sodium expulsion during osmosis upshock are accomplished via secondary transport using the proton gradient as an energy source, and potassium loss during downshock is via a combination of secondary transport and non-specific ion loss through mechanosensitive channels.
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Stability against denaturation mechanisms in halophilic malate dehydrogenase "adapt" to solvent conditions

TL;DR: The solution structure and preferential solvent interactions of hMDH in H2O or 2H2O solvents containing NaCl were studied by densimetry and neutron scattering, and decreasing stability at low temperatures, favouring cold denaturation, was observed.