L. F. S. Mendes

This study shows that Golgi Matrix Proteins (GMPs) tend to form biocondensates via Liquid-Liquid Phase Separation (LLPS) across eukaryotic lineages, suggesting a role for LLPS in Golgi organization.

This study constructs a chimera protein that forms biomolecular condensates with enzymatic activity for degrading polycyclic aromatic hydrocarbons.

This study reconstructs ancestor GRASP proteins to investigate their evolution and role in Golgi ribbon formation and stress-induced secretion.

This study investigates how myristoylation affects GRASP55's membrane anchoring and structural properties using biophysical and computational methods.

This study presents the first high-resolution structure of the GOLD domain of TMED1 and its biophysical properties, revealing dimer formation and insights into its membrane orientation.

This paper investigates the structural flexibility of GRASP PDZ domains and explains their promiscuous interactome through biophysical analysis.

This study investigates the structural properties of human GRASP55 in solution, revealing its disordered regions, monomeric state, and aggregation behavior during denaturation.

The paper shows that the yeast GRASP Grh1 is intrinsically disordered and can form amyloid fibrils, suggesting these properties may be common in the GRASP family.