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Joost Schymkowitz

Joost Schymkowitz

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Biology and Biochemistry
Belgium
2023

D-Index & Metrics

Biology and Biochemistry

D-Index
72
Citations
24711
World Ranking
6169
National Ranking
104

Research.com Recognitions

  • 2023 - Research.com Biology and Biochemistry in Belgium Leader Award

Overview

Joost Schymkowitz is affiliated with KU Leuven in Belgium. Their research spans several fields, primarily within biochemistry, genetics, and molecular biology, along with medicine. Their main areas of study include molecular biology, physiology, materials chemistry, food science, and genetics.

The scientist's contributions focus on topics such as Alzheimer's disease research and treatments, protein structure and dynamics, prion diseases and protein misfolding, enzyme structure and function, proteins in food systems, bacterial genetics and biotechnology, and heat shock proteins research.

Frequent co-authors collaborating with Joost Schymkowitz include:

  • Frédéric Rousseau
  • Nikolaos Louros
  • Bert Houben
  • Rob van der Kant
  • Rodrigo Gallardo

They have published extensively in various venues, notably:

  • bioRxiv (Cold Spring Harbor Laboratory)
  • Nature Communications
  • Bioinformatics
  • Food Hydrocolloids
  • Alzheimer's & Dementia

Selected recent papers from Joost Schymkowitz include:

  • 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

  • Exploring the sequence determinants of amyloid structure using position-specific scoring matrices

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

  • 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

  • The stability effects of protein mutations appear to be universally distributed.

    Nobuhiko Tokuriki;Francois Stricher;Joost Schymkowitz;Luis Serrano

  • 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

  • A graphical interface for the FoldX forcefield

    Joost Van Durme;Javier Delgado;Francois Stricher;Luis Serrano

  • 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

  • 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

  • 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
Sebastian Maurer-Stroh
Sebastian Maurer-Stroh Agency for Science, Technology and Research
Kris Gevaert
Kris Gevaert Ghent University
Marc Cruts
Marc Cruts University of Antwerp
Peter Tompa
Peter Tompa Vrije Universiteit Brussel
Kristel Sleegers
Kristel Sleegers University of Antwerp
Louise C. Serpell
Louise C. Serpell University of Sussex

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