Takashi Ishikawa

The paper identifies complex protein network disruptions in human motile cilia from PCD patients using cryo-ET and proteomics, revealing differences from Chlamydomonas.

This paper enhances the spatial resolution of soft X-ray tomography using physics-aware learning, improving structural fidelity and reducing radiation exposure.

This study evaluates the impact of X-ray radiation doses on cryo-preserved biological samples, showing that high doses do not prevent subsequent cryo-EM analysis for intermediate to high-resolution structural insights.

This paper introduces a self-supervised model to correct missing wedge artifacts in soft X-ray tomography, improving volume quantification and morphology accuracy in cellular structures.

The paper compares proteomic and structural differences in cilia from PCD patients with DNAH5 mutations, showing patient-specific reductions in ciliary components and structural changes in the axoneme.

The paper investigates protein interactions in cilia using CRISPR/CAS9, cryo-ET, and mass spectrometry, revealing a complex involving FAP263, FAP78, FAP184, and FAP151, and links it to dynein f phosphorylation.

The paper uses cryo-electron tomography to study conformational changes in axonemal outer dynein arms during the power stroke cycle, revealing structural differences between states.