L. Brunsveld

Estrogen Receptor alpha/14-3-3 molecular glues as alternative treatment strategy for endocrine resistant breast cancer

This study investigates molecular glues targeting the ER/14-3-3 PPI to overcome endocrine resistance in breast cancer, showing suppression of ER activity and cell proliferation.

Stoichiometric 14-3-3ζ binding promotes phospho-Tau microtubule dissociation and reduces aggregation and condensation

This study shows that 14-3-3ζ binding to phosphorylated Tau reduces its association with microtubules and inhibits aggregation and condensation.

Molecular glues of the regulatory ChREBP/14-3-3 complex protect beta cells from glucolipotoxicity.

This paper identifies molecular glues that stabilize the ChREBP/14-3-3 complex, protecting beta cells from glucolipotoxicity by preventing ChREBP-mediated dedifferentiation.

A Systematic Approach to the Discovery of Protein-Protein Inter-action Stabilizers

This study uses disulfide tethering to identify small molecule stabilizers of 14-3-3{sigma} phospho-peptide interactions, finding selective and efficacious fragments for four of five client complexes.

Early identification of cooperative fragments for protein-protein interaction stabilization

The paper identifies cooperative fragments that stabilize protein-protein interactions using STD NMR and validates their effects through mutagenesis and crystallography.

Macrocycle-stabilization of its interaction with 14-3-3 increases plasma membrane localization and activity of CFTR

This paper identifies a macrocycle that stabilizes the 14-3-3/CFTR complex, enhancing CFTR membrane localization and activity, particularly for the F508del mutation.

A general framework for straightforward model construction of multi-component thermodynamic equilibrium systems

The paper presents a framework for constructing equilibrium models of multi-component systems using reversible reactions, demonstrating simplicity and generality in molecular system analysis.

Molecular basis for inhibition of adhesin-mediated bacterial-host interactions through a novel peptide-binding domain

The paper identifies a peptide-binding domain in a bacterial adhesion protein and develops ligands that inhibit its function, suggesting potential for disrupting harmful bacterial-host interactions.