Brian R. Crane

The paper identifies lysinoalanine crosslinking in the extracellular flagellar hook of Synergistota, expanding the known range of bacteria with this modification beyond spirochetes.

Cache sensor domains of DUF3365/Tll0287 family bind covalent c-type heme through a CXXCH insertion; a signaling member behaves like an NO sensor, a stand-alone one like a redox protein.

This study characterizes SwrD, a protein involved in bacterial flagellar motor regulation, showing it forms hexameric rings and is conserved across spirochetes.

This study investigates how proton-coupled electron transfer and hydrogen bonding modulate radical propagation in proteins, using cytochrome c peroxidase and Zn-porphyrin variants as models.

This study elucidates the signaling mechanism of the E. coli Aer receptor by analyzing its redox-dependent structural changes and their impact on kinase domain conformation.

This paper uses biophysical techniques to show that GT* binding to PDE6 induces a dynamic active state, revealing a previously unobserved conformation associated with catalysis.

The paper identifies a bacterial NO-binding Cache_heme-HAMP receptor that interacts with a Ser/Thr kinase via conserved motifs, revealing a novel mechanism of NO signaling.

This study shows that Porphyromonas gingivalis internalins promote HNSCC metastasis and drug resistance by interacting with E-cadherin and activating signaling pathways.

This paper identifies FlhG, a MinD-like ATPase, as a spatial regulator coupling flagellar assembly to cytokinesis in Borrelia burgdorferi, revealing how spirochetes coordinate flagellation with cell division.

The paper develops an ELISA to screen for protein-protein interaction inhibitors, demonstrating its use in blocking lysinoalanine crosslinking in spirochete flagellar hook proteins.

This study presents the structural dynamics of a multi-domain nitric oxide synthase regulated by a C2 domain using cryoEM, revealing how pterin binding and Ca2+ influence enzyme conformation and activity.

This paper uses ESR spectroscopy to study flavoprotein dynamics in bacterial cells, revealing structural insights and developing a genetically encoded probe for in-cell structural analysis.

This study identifies lactate dehydrogenase (BbLDH) as essential for Borreliella burgdorferi survival and infectivity, and discovers inhibitors targeting this enzyme.

This study identifies two clinically approved small molecules that inhibit lysinoalanine crosslinking in spirochete flagella, reducing bacterial motility and suggesting a new therapeutic approach.

This study identifies MCP5 as essential for Borrelia burgdorferi's immune evasion and transmission, regulated by two signaling pathways.

This study examines how extreme pressure and temperature affect the structure of cytochrome c peroxidase, revealing differences in core, active site, and peripheral regions.

The paper presents the cryo-EM structure of the CRY:TIM complex, revealing molecular mechanisms of circadian clock timing and light entrainment.