Takashi Matsui

The paper identifies a ComQ homolog from Sphaerobacter thermophilus and determines its structural basis for peptide prenylation, revealing insights into the evolution of this modification within the IPPS superfamily.

The paper introduces a 2-ME/DMSO workflow for proteomics that improves quantitative accuracy and reproducibility compared to conventional IAA treatment.

This paper develops a DIA-MS workflow to identify organ-derived peptides in plasma, finding over 2,000 organ-specific peptides including 19 bioactive ones.

This study determines the X-ray crystal structure of SxPT1, a prenyltransferase, and discusses its catalytic mechanism for indole prenylation.

This study determines the cryo-EM structures of two bispecific antibody types and shows that domain linkage rearrangement leads to activity enhancement by altering complex shape and dynamics.

This paper introduces a method using 2-mercaptoethanol and DMSO to specifically modify cysteine residues, reducing offsite modifications in proteome analysis.