F
Francois-Xavier Theillet
Researcher at Leibniz Association
Publications - 22
Citations - 1945
Francois-Xavier Theillet is an academic researcher from Leibniz Association. The author has contributed to research in topics: Nuclear magnetic resonance spectroscopy & Phosphorylation. The author has an hindex of 14, co-authored 18 publications receiving 1572 citations. Previous affiliations of Francois-Xavier Theillet include Max Planck Society & National Scientific and Technical Research Council.
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Journal ArticleDOI
Structural disorder of monomeric α-synuclein persists in mammalian cells
Francois-Xavier Theillet,Francois-Xavier Theillet,Andres Binolfi,Andres Binolfi,Beata Bekei,Andrea Martorana,Honor May Rose,Marchel Stuiver,Silvia Verzini,Dorothea Lorenz,Marleen van Rossum,Daniella Goldfarb,Philipp Selenko +12 more
TL;DR: It is established that different types of crowded intracellular environments do not inherently promote α-synuclein oligomerization and, more generally, that intrinsic structural disorder is sustainable in mammalian cells.
Journal ArticleDOI
The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins.
Francois-Xavier Theillet,Lajos Kalmar,Peter Tompa,Kyou-Hoon Han,Philipp Selenko,A. Keith Dunker,Gary W. Daughdrill,Vladimir N. Uversky +7 more
TL;DR: This review is the first in a series of publications dedicated to the roles that different amino acid residues play in defining the phenomenon of protein intrinsic disorder.
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Disorder and residual helicity alter p53-Mdm2 binding affinity and signaling in cells
Wade Borcherds,Francois-Xavier Theillet,Andrea Katzer,Ana Finzel,Katie M. Mishall,Anne Terese Powell,Hongwei Wu,Wanda Manieri,Christoph Dieterich,Philipp Selenko,Alexander Loewer,Gary W Daughdrill +11 more
TL;DR: It is shown that increasing residual p53 helicity results in stronger Mdm2 binding, altered p53 dynamics, impaired target gene expression and failure to induce cell cycle arrest upon DNA damage, establishing that residual structure is an important determinant of signaling fidelity in cells.
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Cell signaling, post-translational protein modifications and NMR spectroscopy
Francois-Xavier Theillet,Caroline Smet-Nocca,Stamatios Liokatis,Rossukon Thongwichian,Jonas Kosten,Mi-Kyung Yoon,Richard W. Kriwacki,Isabelle Landrieu,Guy Lippens,Philipp Selenko +9 more
TL;DR: The previously uncharacterized NMR properties of lysine propionylation, butyrylation, succinylation, malonylation and crotonylation are delineated to define an initial reference frame for comprehensive PTM studies by high-resolution NMR spectroscopy.
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Bacterial in-cell NMR of human α-synuclein: a disordered monomer by nature?
TL;DR: In-cell NMR evidence obtained directly in intact Escherichia coli cells is provided that challenges a tetrameric conformation under native in vivo conditions and indicates clearly that inside E. coli α-synuclein is mostly monomeric and disordered.