Miklós Guttman

This study shows HSPB1 and HSPB5 use distinct N-terminal regions to delay tau aggregation, with HSPB1 under normal conditions and HSPB5 under stress.

The paper measures conformational fluctuations of protein domains using hydrogen-deuterium exchange mass spectrometry and uses computational modeling to design mutations that stabilize low-stability segments.

This study examines how phosphorylation at different sites in HSPB5 affects its oligomeric structure and function, revealing distinct cellular outcomes based on the extent of phosphorylation.

This study uses pulsed HDX-MS to investigate whether tau4RD fibril polymorphism is imprinted during early aggregation or arises from structural rearrangements later in the process.

The paper introduces pyHXExpress, a tool for automated HDX-MS analysis, validated on synthetic data to detect multimodality and characterize protein dynamics.

This study identifies a type-specific B cell epitope on OspC type A of Borreliella burgdorferi and shows its role in antibody-mediated motility inhibition.

This study reveals how two F-box proteins, FBXO22 and FBXL17, recognize distinct structural features of the BACH1 BTB dimer under oxidative stress, leading to its ubiquitination and degradation.

This study determines the structure of a human monoclonal antibody in complex with OspC from Borreliella burgdorferi, revealing its epitope and interaction mechanism.

The paper identifies tryptanthrin analogs as potent substoichiometric inhibitors of tau4RD aggregation, showing low nanomolar potency and demonstrating structure-activity relationship principles for tau targeting.