Andrea Balbo

Imaging brain phospholipase A2 activation in awake rats in response to the 5-HT2A/2C agonist (+/-)2,5-dimethoxy-4-iodophenyl-2-aminopropane (DOI).

Combined affinity and rate constant distributions of ligand populations from experimental surface binding kinetics and equilibria.

Imaging of brain serotonergic neurotransmission involving phospholipase A2 activation and arachidonic acid release in unanesthetized rats.

Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition.

Studying multiprotein complexes by multisignal sedimentation velocity analytical ultracentrifugation.

Altered signaling pathways underlying abnormal hippocampal synaptic plasticity in the Ts65Dn mouse model of Down syndrome.

Using prior knowledge in the determination of macromolecular size-distributions by analytical ultracentrifugation.

Cellular expression and crystal structure of the murine cytomegalovirus major histocompatibility complex class I-like glycoprotein, m153.

Extended polypeptide linkers establish the spatial architecture of a pyruvate dehydrogenase multienzyme complex.

Measuring protein-protein interactions by equilibrium sedimentation.

Characterizing protein-protein interactions by sedimentation velocity analytical ultracentrifugation.

A bayesian approach for quantifying trace amounts of antibody aggregates by sedimentation velocity analytical ultracentrifugation.

Autoinhibition of Arf GTPase-activating protein activity by the BAR domain in ASAP1.

The C-terminal domain of Plasmodium falciparum merozoite surface protein 3 self-assembles into alpha-helical coiled coil tetramer.

On the analysis of sedimentation velocity in the study of protein complexes.

Accounting for solvent signal offsets in the analysis of interferometric sedimentation velocity data.

Cooperative interactions at the SLP-76 complex are critical for actin polymerization.

Macromol. Biosci. 7/2010.

The boundary structure in the analysis of reversibly interacting systems by sedimentation velocity.

Dimeric states of neural- and epithelial-cadherins are distinguished by the rate of disassembly.

Density contrast sedimentation velocity for the determination of protein partial-specific volumes.