Wataru Shihoya

This study determines the cryo-EM structure of SfApuR2, an ultraviolet-sensitive anion-conducting rhodopsin, and identifies structural features that explain its UV sensitivity and gating mechanism.

This study determines the cryo-EM structure of GPR30 with bicarbonate ions, identifies key residues for activation, and provides insights into G-protein coupling and drug development.

The paper identifies widespread xanthorhodopsin genes in cyanobacteria and characterizes a unique variant from an Antarctic cyanobacterium that binds hydroxylated lutein, enhancing light-harvesting efficiency in extreme environments.

This study identifies ACE2 diversity in horseshoe bats and shows bidirectional evolutionary shaping between ACE2 and sarbecovirus spike proteins.

The paper reports cryo-EM structures of two methanogenic Schizorhodopsins, revealing distinct proton transport mechanisms and structural adaptations for thermal stability.

This study investigates the ACE2 tropism of sarbecoviruses across 17 mammals using pseudovirus assays, structural analysis, and phylogenetics to identify genetic factors influencing host range.

The paper reports the cryo-EM structure of a blue-shifted channelrhodopsin from Klebsormidium nitens and develops mutants with blue-shifted action spectra.

The paper reports light energy transfer from hydroxylated carotenoids to heimdallarchaeial rhodopsins in marine archaea, showing light-harvesting capabilities in archaea similar to bacterial rhodopsins.

This study investigates ligand promiscuity and signaling bias in chemokine receptors by analyzing binding modes and determining cryo-EM structures of receptor-ligand complexes.

The paper identifies a novel A3R-selective ligand and reveals structural insights into A3R activation, enabling structure-guided engineering of m6A-insensitive A3R for drug discovery.

This study investigates how ETB couples to different G proteins, finding that it interacts with Gi and Gq but not Gs, with specific regions influencing these interactions.

The paper reports cryo-EM structures of the ETB receptor bound to the lasso peptide RES-701-3, revealing its inverse agonist mechanism through hydrophobic interactions and conformational stabilization.

The paper identifies m6A as an endogenous ligand for the A3 adenosine receptor, showing it has higher affinity than unmodified adenosine and plays a role in type I allergy.

The paper presents cryo-EM structures of CALHM channels from different species, revealing their ATP conduction and oligomerization mechanisms.

The paper presents a cryo-EM structure of the human PAC1 receptor bound to PACAP and an engineered Gs heterotrimer, revealing functional differences in the ECD between PAC1R and GLP1R.

The paper reports X-ray structures of the human ETB receptor bound to agonists, revealing molecular mechanisms of activation and partial agonism.