Frédéric Rousseau

ORCID: 0000-0002-9189-7399
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About
Contact & Profiles
Research Areas
  • Protein Structure and Dynamics
  • Alzheimer's disease research and treatments
  • Enzyme Structure and Function
  • RNA and protein synthesis mechanisms
  • Prion Diseases and Protein Misfolding
  • Machine Learning in Bioinformatics
  • Estrogen and related hormone effects
  • Chemical Synthesis and Analysis
  • Steroid Chemistry and Biochemistry
  • Bacterial Genetics and Biotechnology
  • Heat shock proteins research
  • Monoclonal and Polyclonal Antibodies Research
  • Bioinformatics and Genomic Networks
  • Computational Drug Discovery Methods
  • RNA Research and Splicing
  • X-ray Diffraction in Crystallography
  • Amyotrophic Lateral Sclerosis Research
  • Cellular transport and secretion
  • Proteins in Food Systems
  • Crystallization and Solubility Studies
  • Agriculture and Rural Development Research
  • Cancer-related Molecular Pathways
  • Glycosylation and Glycoproteins Research
  • Ubiquitin and proteasome pathways
  • Endoplasmic Reticulum Stress and Disease

KU Leuven
2016-2025

VIB-KU Leuven Center for Brain & Disease Research
2016-2025

Switch
2008-2024

Rega Institute for Medical Research
2024

Institut de Radioprotection et de Sûreté Nucléaire
2023-2024

Vlaams Instituut voor Biotechnologie
2006-2021

VIB-KU Leuven Center for Microbiology
2021

Concordia University
2021

Institut de Recherche Interdisciplinaire en Sciences Sociales
2009-2017

Center for Research and Interdisciplinarity
2009-2017

Liquid-liquid phase separation (LLPS) of RNA-binding proteins plays an important role in the formation multiple membrane-less organelles involved RNA metabolism, including stress granules. Defects granule homeostasis constitute a cornerstone ALS/FTLD pathogenesis. Polar residues (tyrosine and glutamine) have been previously demonstrated to be critical for ALS-linked proteins. We now identify active arginine-rich domains these separations. Moreover, dipeptide repeats (DPRs) derived from...

10.1016/j.molcel.2017.02.013 article EN cc-by-nc-nd Molecular Cell 2017-03-01

The empirical force field Fold-X was developed previously to allow rapid free energy calculations in proteins. Here, we present an enhanced version of the allowing prediction position structural water molecules and metal ions, together called single atom ligands. picks up 76% found interact with two or more polar atoms proteins high-resolution crystal structures predicts their within 0.8 Å on average. ion-binding sites have success rates between 90% 97% depending metal, overall standard...

10.1073/pnas.0501980102 article EN Proceedings of the National Academy of Sciences 2005-07-08

A graphical user interface for the FoldX protein design program has been developed as a plugin YASARA molecular graphics suite. The most prominent commands such free energy difference upon mutagenesis and interaction calculations can now be run entirely via windowed menu system results are immediately shown on screen.The is written in Python freely available download at http://foldxyasara.switchlab.org/ supported Linux, MacOSX MS Windows.

10.1093/bioinformatics/btr254 article EN Bioinformatics 2011-04-19

Abstract Hexanucleotide repeat expansions in C9orf72 are the most common cause of amyotrophic lateral sclerosis (ALS) and frontotemporal degeneration (FTD) (c9ALS/FTD). Unconventional translation these repeats produces dipeptide proteins (DPRs) that may neurodegeneration. We performed a modifier screen Drosophila discovered critical role for importins exportins, Ran-GTP cycle regulators, nuclear pore components arginine methylases mediating DPR toxicity. These findings provide evidence an...

10.1038/srep20877 article EN cc-by Scientific Reports 2016-02-12

Abnormal calcium signaling is a central pathological component of Alzheimer's disease (AD). Here, we describe the identification class compounds called ReS19-T, which are able to restore homeostasis in cell-based models tau pathology. Aberrant accumulation leads uncontrolled activation store-operated channels (SOCCs) by remodeling septin filaments at cell cortex. Binding ReS19-T septins restores filament assembly state and restrains entry through SOCCs. In amyloid-β tau-driven mouse disease,...

10.1126/science.add6260 article EN Science 2024-05-30

Recalcitrant bacterial infections can be caused by various types of dormant bacteria, including persisters and viable but nonculturable (VBNC) cells. Despite their clinical importance, we know fairly little about dormancy development recovery. Previously, established a correlation between protein aggregation in Escherichia coli. Here, present further support for direct relationship both. Our experiments demonstrate that aggregates progressively sequester proteins involved energy production,...

10.1038/s41467-025-56387-8 article EN cc-by-nc-nd Nature Communications 2025-01-26

Since the reformulation of amyloid cascade hypothesis to focus on oligomeric aggregates beta as prime toxic species causing Alzheimer's disease, many researchers refocused detecting a specific molecular assembly defined size thatis main trigger disease. The result has been identification host assemblies containing from two up hundred molecules peptide, which were all found impair memory formation in mice. This clearly demonstrates that is insufficient define toxicity and peptide conformation...

10.1186/alzrt36 article EN cc-by Alzheimer s Research & Therapy 2010-01-01

<h3>Objective:</h3> To assess the genetic contribution of <i>TBK1</i>, a gene implicated in amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and FTD-ALS, Belgian FTD ALS patient cohorts containing significant part genetically unresolved patients. <h3>Methods:</h3> We sequenced <i>TBK1</i> hospital-based cohort 482 unrelated patients with FTD-ALS 147 an extended family DR158. followed up mutation carriers by segregation studies, transcript protein expression analysis,...

10.1212/wnl.0000000000002220 article EN cc-by-nc-nd Neurology 2015-11-19
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