Joost W. H. Schymkowitz

The paper introduces WhatRes, a tool to evaluate AI-predicted protein structures by comparing their geometry to experimental structures across resolution and realism.

The paper identifies two polymorphs of an independent amyloid core in the C-terminal region of medin, showing it has multiple aggregation-prone regions.

The paper uses proteomics to show increased ECM remodeling and complement activation in cardiac ATTR amyloidosis.

The paper uses energetic profiling on cryo-EM data to uncover thermodynamic principles governing amyloid fibril maturation and polymorphic divergence.

Amyloid Explorer provides a standardized, thermodynamically annotated atlas of amyloid fibril structures, revealing conserved assembly rules and enabling mechanistic insights.

This study shows human macrophages and microglia actively produce Aβ42 fibrils, which seed amyloid plaques and tau aggregation, and this process is influenced by genetic factors like TREM2.

This study determines the cryo-EM structures of Aβ40 and medin fibrils in vitro, revealing polymorphic remodeling and mixed amyloid interactions.

This study introduces FoldDelay, a metric quantifying protein folding delays during translation, showing its correlation with misfolding and aggregation risks.

This paper designs IL2 muteins with enhanced Treg or CD8 T cell specificity and improved production by predicting mutations using SolubiS and testing their functional and structural properties.

This paper introduces EvolveX, a computational pipeline for designing stable single-domain antibodies with high affinity, demonstrating improved binding affinity to human targets.

The paper introduces MadraX, a differentiable force field implemented as a PyTorch module to enable end-to-end integration with deep learning algorithms in structural biology.

This study shows N-glycosylation prevents protein aggregation by steric hindrance, especially in proteins prone to misfolding, using computational and biochemical analyses.

This paper analyzes amyloid polymorphism structure to explain disease-related stability and polymorphic bias, identifying conserved structural frameworks and templating interactions that influence cellular vulnerability.

The paper shows how EndophilinA couples calcium influx to synaptic autophagy and identifies a Parkinson-risk mutation that disrupts this process.

This study shows heterotypic interactions between Aβ APRs and homologous protein segments accelerate Aβ assembly, alter fibril morphology, and are enriched in AD plaques but not in mouse models.

The paper shows viral ligand-receptor interactions enhance the spread of protein misfolding via extracellular vesicles and direct cell contact.

The paper identifies MOAG-4/SERF as modifiers of amyloid formation through charge complementation, showing that charge interactions drive protein aggregation and toxicity.