Koji Ogawa

TL;DR: A targeted proteomics platform—in vitro proteome–assisted multiple reaction monitoring (MRM) for proteinabsolute quantification (iMPAQT) by using >18,000 human recombinant proteins, thus enabling protein absolute quantification on a genome-wide scale.

TL;DR: Structural information obtained with NMR analysis revealed that Col003 competitively binds to the collagen-binding site on Hsp47, and it is proposed that these structural insights could provide a basis for designing more effective therapeutic drugs for managing fibrosis.

TL;DR: The combination of in vitro display evolution of cyclized N-alkyl peptidomimetics and in vitro expression of human proteins would be a powerful approach for the high-speed discovery of diverse human protein-targeted cyclized EMTs, as well as identifying a novel β-catenin-binding cyclized peptoid-peptide chimera.

TL;DR: Using the DIVERSE system, de novo creation of non-enzymatically covalent-labeling peptide tags for a synthetic small-molecule target from a random peptide library was demonstrated and protein labeling with these tags was applicable to N- and C-terminal fusions, multiple different proteins and fluorophores, and intracellular labeling.

TL;DR: The Warburg effect appeared in absolute protein levels between tumor and normal mucosa specimens demonstrated, and the levels of proteins associated with the tricarboxylic citric acid cycle were remarkably reduced in the malignant tumors which had relapsed after surgery and treatment with 5‐fluorouracil‐based adjuvant therapy.