Siavash Vahidi

This study uses charge detection mass spectrometry to analyze DegP oligomerization states and client interactions, revealing new oligomer types and dynamic behavior.

This study uses cryo-EM and charge detection mass spectrometry to determine the stoichiometry and structure of Bpa-substrate complexes in Mtb, revealing an undecameric apo form and a Bpa12:HspR2 complex.

This paper demonstrates positive cooperativity between subunits in the M. tuberculosis 20S proteasome core particle by using a hybrid subunit assembly and isotopic-coding strategy to resolve symmetry-masked allostery.

This study determines the structure and mechanism of UbK1, a bacterial kinase in P. gingivalis, identifies PorX as a noncanonical substrate, and shows UbK1's role extends beyond canonical secretion pathways.

The paper determines the structural basis of substrate recognition by PafA, showing that broad specificity arises from dynamic, geometrically compatible interactions rather than sequence-specific binding.

This paper introduces a universal volatile buffer system using fluorinated ethylamines for native LC-MS analysis of antibody-based therapeutics, enabling broad pH range buffering and compatibility with mass spectrometry.

This study defines the temperature-sensitive oligomerization mechanism of Bpa and elucidates its interaction with a surrogate substrate using biophysical techniques.

HDgraphiX visualizes HDX-MS data using statistical analysis and generates publication-quality plots and structural maps.

This study reveals the activation mechanism of human mitochondrial ClpP protease through structures showing how inhibitors induce an allosteric transition to the active state, with implications for cancer therapy.

The paper presents the first high-resolution structure of Mycobacterium tuberculosis 20S core particle in an inactive state, revealing the structural basis for allosteric regulation.

This study uses HDX-MS to investigate the oligomeric states and conformational dynamics of PafA, revealing its monomeric and dimeric forms and how nucleotide binding affects its structure and function.

This study investigates how nucleotide binding and Zn²⁺ affect the conformational dynamics and allosteric regulation of the YME1L protease catalytic domain.