Zoltán Gáspári

The paper investigates how two autism-associated mutations in the Homer1 EVH1 domain affect its internal dynamics and binding properties using experimental and computational methods.

The paper introduces a method to determine the size of solute particles, specifically postsynaptic proteins, using diffusion in microfluidic environments and fluorescent labeling.

The paper shows that a hexameric complex of GKAP and LC8 proteins has constrained stoichiometry with retained flexibility in the linker region.

The paper investigates how missense mutations in Shank1 PDZ domain affect ligand-specific binding affinity through dynamic interactions.

This study presents an atomistic model of full-length Homer1 tetramer and NMR structure of its EVH1 domain, revealing ligand-induced conformational changes and dynamic regions in the coiled coil.

The paper models the effects of a hypomorphic Shank mutation on protein complex formation in postsynaptic densities, showing that mutation impacts depend on protein availability and cell type.

The paper identifies charged sequence motifs in proteins that are associated with liquid-liquid phase separation, with alternating charge patterns showing the strongest association.

PSINDB compiles postsynaptic protein-protein interactions with structural and biological details, providing a resource for neurobiology research.

This study develops a pipeline to analyze the cistrome of human postsynaptic density using ChIP-seq data and transcription factor information, finding correlations between co-regulation and protein complex formation.

The paper analyzes disease-causing germline mutations in coiled-coil structures and finds that N-terminal residues are critical for superhelix assembly and folding.

The paper investigates how ligand binding affects intra- and inter-domain motions in the PSD-95 PDZ12 tandem, revealing a key regulatory role for the β2-β3 loop.

The paper analyzes the structural features of postsynaptic proteins to show that their combination of ordered and disordered regions enables diverse interactions crucial for learning and memory.

The paper uses molecular dynamics simulations and NMR parameters to study ligand binding in gastrotropin, revealing two distinct barrel opening modes and partial unfolding during the process.