M
Marlène Martinho
Researcher at Aix-Marseille University
Publications - 41
Citations - 1955
Marlène Martinho is an academic researcher from Aix-Marseille University. The author has contributed to research in topics: Site-directed spin labeling & Electron paramagnetic resonance. The author has an hindex of 24, co-authored 38 publications receiving 1666 citations. Previous affiliations of Marlène Martinho include University of Évry Val d'Essonne & University of Marburg.
Papers
More filters
Journal ArticleDOI
Role of Tau as a Microtubule-Associated Protein: Structural and Functional Aspects.
Pascale Barbier,Orgeta Zejneli,Marlène Martinho,Alessia Lasorsa,Valérie Belle,Caroline Smet-Nocca,Philipp O. Tsvetkov,François Devred,Isabelle Landrieu +8 more
TL;DR: Since destabilization of MTs after dissociation of Tau could contribute to toxicity in neurodegenerative diseases, a molecular understanding of this interaction and its regulation is essential.
Journal ArticleDOI
A Synthetic High‐Spin Oxoiron(IV) Complex: Generation, Spectroscopic Characterization, and Reactivity
Jason England,Marlène Martinho,Erik R. Farquhar,Jonathan R. Frisch,Emile L. Bominaar,Eckard Münck,Lawrence Que +6 more
TL;DR: High versus low: The high-yield generation of a synthetic high-spin oxoiron(IV) complex, [Fe(IV)(O)(TMG(3)tren)](2+) (see picture), has been achieved by using the very bulky tetradentate TMG(3), in order to both sterically protect the oxo iron moiety and enforce a trigonal bipyramidal geometry at the iron center.
Journal ArticleDOI
Proton- and reductant-assisted dioxygen activation by a nonheme iron(II) complex to form an oxoiron(IV) intermediate.
Aurore Thibon,Jason England,Marlène Martinho,Victor G. Young,Jonathan R. Frisch,Régis Guillot,Jean Jacques Girerd,Eckard Münck,Lawrence Que,Frédéric Banse +9 more
TL;DR: Enzymes with an iron(III) resting state often require a tetrahydropterin or an α-keto acid cofactor to form an FeIV(O) intermediate, and such intermediates have recently been trapped and characterized for several enzymes.
Journal ArticleDOI
Thermal Unfolding of Proteins Probed at the Single Molecule Level Using Nanopores
Linda Payet,Marlène Martinho,Manuela Pastoriza-Gallego,Jean-Michel Betton,Loïc Auvray,Juan Pelta,Juan Pelta,Jérôme Mathé +7 more
TL;DR: The thermal unfolding of a protein is studied, probed by two protein nanopores: aerolysin and α-hemolysin, and a similar sigmoid function fits the normalized event frequency evolution for both nanopores, thus the unfolding curve does not depend on the structure and the net charge of the nanopore.
Journal ArticleDOI
Human deoxyhypusine hydroxylase, an enzyme involved in regulating cell growth, activates O2 with a nonheme diiron center
Van V. Vu,Joseph P. Emerson,Joseph P. Emerson,Marlène Martinho,Yeon Sook Kim,Yeon Sook Kim,Eckard Münck,Myung Hee Park,Lawrence Que +8 more
TL;DR: Spectroscopic results presented herein provide direct spectroscopic evidence that hDOHH has an antiferromagnetically coupled diiron center with histidines and carboxylates as likely ligands, as suggested by mutagenesis experiments.