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Frederic Rousseau

Frederic Rousseau

D-Index & Metrics

Biology and Biochemistry

D-Index
71
Citations
23998
World Ranking
6535
National Ranking
113

Overview

Frederic Rousseau is a researcher affiliated with KU Leuven in Belgium, contributing extensively to the fields of biochemistry, genetics, and molecular biology, as well as medicine. Their work spans a wide array of subfields including molecular biology, physiology, materials chemistry, food science, and genetics.

Their research primarily focuses on topics such as Alzheimer's disease research and treatments, protein structure and dynamics, prion diseases and protein misfolding, enzyme structure and function, crystallization and solubility studies, X-ray diffraction in crystallography, and proteins in food systems.

Frederic Rousseau has coauthored publications with several frequent collaborators, including Joost Schymkowitz, Nikolaos Louros, Bert Houben, Rob van der Kant, and Rodrigo Gallardo.

They have contributed numerous papers to a variety of scientific venues, with frequent appearances in bioRxiv (Cold Spring Harbor Laboratory), Nature Communications, The Cambridge Structural Database, Bioinformatics, and Food Hydrocolloids.

Among Rousseau's recent papers are:

  • Mechanisms and pathology of protein misfolding and aggregation (2023, Nature Reviews Molecular Cell Biology)
  • A guide to studying protein aggregation (2021, FEBS Journal)
  • Medin co-aggregates with vascular amyloid-β in Alzheimer's disease (2022, Nature)
  • Structure-based machine-guided mapping of amyloid sequence space reveals uncharted sequence clusters with higher solubilities (2020, Nature Communications)
  • Repurposing the Antidepressant Sertraline as SHMT Inhibitor to Suppress Serine/Glycine Synthesis-Addicted Breast Tumor Growth (2020, Molecular Cancer Therapeutics)

Best Publications

  • The FoldX web server: an online force field

    Joost Schymkowitz;Jesper Borg;Francois Stricher;Robby Nys

  • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins

    Ana-Maria Fernandez-Escamilla;Frederic Rousseau;Joost Schymkowitz;Luis Serrano

  • Protein Phase Separation: A New Phase in Cell Biology.

    Steven Boeynaems;Steven Boeynaems;Simon Alberti;Nicolas L. Fawzi;Tanja Mittag

  • Neurotoxicity of Alzheimer's disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio.

    Inna Kuperstein;Kerensa Broersen;Kerensa Broersen;Iryna Benilova;Iryna Benilova;Iryna Benilova;Jef Rozenski

  • The mechanism of γ-Secretase dysfunction in familial Alzheimer disease

    Lucía Chávez-Gutiérrez;Leen Bammens;Iryna Benilova;Annelies Vandersteen;Annelies Vandersteen

  • Phase Separation of C9orf72 Dipeptide Repeats Perturbs Stress Granule Dynamics

    Steven Boeynaems;Elke Bogaert;Denes Kovacs;Albert Konijnenberg

  • Protein aggregation and amyloidosis: confusion of the kinds?

    Frederic Rousseau;Joost Schymkowitz;Luis Serrano

  • Gain of function of mutant p53 by coaggregation with multiple tumor suppressors

    Jie Xu;Joke Reumers;José R Couceiro;Frederik De Smet

  • A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins.

    Rune Linding;Joost Schymkowitz;Frederic Rousseau;Francesca Diella

  • Prediction of water and metal binding sites and their affinities by using the Fold-X force field

    Joost W. H. Schymkowitz;Frederic Rousseau;Ivo C. Martins;Jesper Ferkinghoff-Borg

  • Lipids revert inert Aβ amyloid fibrils to neurotoxic protofibrils that affect learning in mice

    Ivo Cristiano Martins;Inna Kuperstein;Hannah Wilkinson;Elke Maes

  • How evolutionary pressure against protein aggregation shaped chaperone specificity

    Frederic Rousseau;Luis Serrano;Joost W.H. Schymkowitz

  • The unfolding story of three-dimensional domain swapping.

    Frederic Rousseau;Joost W.H. Schymkowitz;Laura S. Itzhaki

  • Restricted Location of PSEN2/γ-Secretase Determines Substrate Specificity and Generates an Intracellular Aβ Pool

    Ragna Sannerud;Cary Esselens;Paulina Ejsmont;Rafael Mattera

  • SNPeffect 4.0: on-line prediction of molecular and structural effects of protein-coding variants

    Greet De Baets;Joost J. J. van Durme;Joke Reumers;Sebastian Maurer-Stroh

  • Drosophila screen connects nuclear transport genes to DPR pathology in c9ALS/FTD

    Steven Boeynaems;Elke Bogaert;Emiel Michiels;Ilse Gijselinck

  • Structural Basis for Increased Toxicity of Pathological Aβ42:Aβ40 Ratios in Alzheimer Disease

    Kris Pauwels;Thomas L. Williams;Kyle L. Morris;Wim Jonckheere;Wim Jonckheere

  • Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues

    Frederic Rousseau;Joost Schymkowitz;Hannah Wilkinson;L.s. Itzhaki

  • PupaSuite: finding functional single nucleotide polymorphisms for large-scale genotyping purposes

    Lucía Conde;Juan M. Vaquerizas;Hernán Dopazo;Leonardo Arbiza

  • Exploring the sequence determinants of amyloid structure using position-specific scoring matrices (vol 7, pg 237, 2010)

    Sebastian Maurer-Stroh;Maja Debulpaep;Nico Kuemmerer;Manuela Lopez de la Paz

Frequent Co-Authors

Luis Serrano
Luis Serrano Centre for Genomic Regulation
Marc Cruts
Marc Cruts University of Antwerp
Peter Tompa
Peter Tompa Vrije Universiteit Brussel
Kris Gevaert
Kris Gevaert Ghent University
Kristel Sleegers
Kristel Sleegers University of Antwerp
Christine Van Broeckhoven
Christine Van Broeckhoven University of Antwerp

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