Shinya Tsukiji

TL;DR: Data establish LDT chemistry as a new tool for the study and manipulation of biological systems as well as for constructing a biosensor directly inside cells without genetic engineering.

TL;DR: This article outlines the technique, sortase‐mediated ligation, and its applications in protein engineering, which include the introduction of unnatural molecules into proteins, protein immobilization, protein–protein conjugation, protein cyclization, as a self‐cleavable tag for protein expression, protein-PNA hybrids, neoglycoconjugates, and cell‐surface protein labeling, etc.

TL;DR: The use of supramolecular organic nanoparticles to detect specific proteins by (19)F-based MRI in an off/on mode with recognition-driven disassembly of nanoprobes for a turn-on ( 19)F signal is unprecedented and may extend the use of (19]F MRI for specific protein imaging.

TL;DR: A general strategy for the site‐specific modification of cell surface proteins with synthetic molecules by using Sortase, a transpeptidase from Staphylococcus aureus is described, which provides a powerful tool for cell biology and cell surface engineering.

TL;DR: It was clearly demonstrated by biochemical analyses that the target-selective labeling of Congerin II, an animal lectin having selective affinity for Lactose/LacNAc (N-acetyllactosamine), was achieved in the presence of Lac-tethered DMAPs and acyl donors containing probes such as fluorescent molecules or biotin.