Nicolas Lux Fawzi

Short UG-rich RNAs bind and stabilize TDP-43 RNA-recognition motifs to allosterically destabilize its prion-like domain helical region, preventing aggregation and mitigating neurodegeneration in cells and mice.

This study uses NMR spectroscopy to show that FUS condensates cause partial unfolding of TERRA RNA G-quadruplexes, suggesting phase-separated environments modulate RNA structure.

This study introduces β-sheet breaking proline residues into FUS prion-like domain to prevent aggregation and toxicity while preserving phase separation and function.

This study identifies the glycine-arginine-rich motif of 53BP1 as essential for RNA interactions and phase separation during DNA damage response, showing its role in DNA repair.

This paper investigates how the disordered C-terminal domain of TDP-43 interacts with RNA and identifies key residues and structural features that mediate RNA recognition and binding specificity.

This study shows methionine oxidation in TDP-43's C-terminal domain disrupts structure and phase separation through region-specific mechanisms.

This study shows RNA modulates FUS condensate assembly and aggregation through specific molecular interactions, affecting phase separation and aggregate formation.

This study investigates the structural basis of TDP-43 C-terminal domain multimerization using biophysical experiments, AlphaFold2-Multimer, and simulations, revealing helical oligomerization and the role of specific residues in phase separation and disease.

AlphaFlex generates atomistic conformational ensembles for human proteins with intrinsically disordered regions, integrating AlphaFold models and implicit bilayers for transmembrane proteins.

This study shows that TDP-43 aggregation in stress granules requires up-concentration and oxidative stress, leading to intra-condensate demixing and pathological aggregates.

The paper identifies lipoamide as a small molecule that dissolves stress granules and improves outcomes in ALS models by modulating redox-sensitive proteins.

The paper expands the molecular grammar of polar residues and arginine in FUS prion-like domain phase separation and aggregation by showing additional residues contribute to these processes.

The paper shows CLAMP, a DNA-binding factor, regulates sex-specific splicing by interacting with RNA and modulating RBP dynamics.

The paper shows that CLAMP and Zelda work together to drive zygotic genome activation in Drosophila by enhancing chromatin accessibility and promoting transcription.

The paper identifies that FXR2P's low complexity domain forms distinct fibrils with different ribosome associations, requiring collaboration with its RNA binding domain.