A. Raasakka

The paper characterizes the disordered structure and functional properties of the HNF-1A transactivation domain using bioinformatics and biophysical methods.

This study links AlphaFold2 predictions of myelin-specific intrinsically disordered proteins to experimental data, showing helical segments in predicted models match membrane-binding sites.

This study determines the structure of human myelin proteolipid protein (PLP) and its isoform DM20, revealing their dimeric conformation and role in membrane stacking and organization.

This study investigates the structural and biochemical effects of CMT-linked GDAP1 mutations, finding reduced thermal stability and disrupted interaction networks that may impair neuronal function.

This study structurally and biophysically characterizes HNF-1A variants associated with MODY3 diabetes, showing reduced functionality in three variants compared to wild-type.

This study produces and characterizes high-affinity anti-Arc nanobodies, revealing structural dynamics of Arc CTD and its role in oligomerization and capsid formation.

The paper determines the crystal structure of the human GDAP1 core domain, identifies a fatty acid ligand, and reveals structural insights into disease-related mutations and oligomerization.

The paper determines the 3D structure of human P4H-TM using X-ray crystallography, revealing structural features and Ca2+ binding properties relevant to its catalytic activity and association with HIDEA syndrome.

The paper determines the crystal structure of mouse CSAD, identifies substrate specificity determinants, and shows open/close motions in solution.

This study determines the crystal structure of the AnxA11 core, identifies a stabilizing N-terminal segment, and links three ALS mutations to conserved arginine residues critical for annexin folding.

This study uses structural and functional analyses to reveal how myelin protein P2 forms a supramolecular lattice between lipid bilayers, identifying key residues and interactions involved in membrane binding.

This study investigates how neuropathy-related mutations in the cytoplasmic tail of the human myelin protein P0 affect its membrane binding properties and function.

This study investigates how ionic strength and calcium influence the membrane interactions of myelin basic protein and the cytoplasmic domain of P0, showing their impact on lipid vesicle aggregation.

This study characterizes the molecular structure and function of myelin protein P0, showing how its extracellular domains stack lipid membranes and stabilize the intraperiod line in peripheral myelin.