A paper on our phosphorylation analysis service was published in a leading international academic journal

The results of our previously reported (our “News” dated 12/23/2024) collaborative study with Prof. Steven Grant of Virginia Commonwealth University have been published in the February 10, 2025 issue of Signal Transduction and Targeted Therapy [Impact Factor (IF) 40.8] dated February 10, 2025 (https://www.nature.com/articles/s41392-025-02125-x).
Under the guidance of Professor Grant, we contributed to elucidating the mechanism of synergistic effects of the combination of two existing drugs in acute myeloid leukemia (AML) based on changes in the phosphorylation states of intracellular molecules. This study was the first application of our improved phosphorylation array service (#1), which enables the measurement of phosphorylation by serine/threonine kinases in addition to tyrosine kinases.

#1 Our phosphorylation analysis service and its improvements
“Phospho-Totum” (Patent No. 6884389), a phosphorylation analysis system, is the world’s first system that seamlessly integrates comprehensive measurement of phosphorylation state in cells and data analysis. It comprehensively measures the phosphorylation levels of 1,471 proteins (substrates) spotted on glass plates (arrays) in accordance with the activation level of kinases in cell or tissue lysate in a one-time experiment. From these measurements, the activation level of pathways, kinases, and target kinases of drug candidates are estimated using a computational platform equipped with a proprietary set of algorithms.
This is different from the residue-by-residue measurement/analysis of substrates that is usually associated with the term “phosphorylation measurement/analysis. This system measures the phosphorylation level of an entire protein and estimates the activation of kinases and pathways that link the protein to its phosphorylation at a macroscopic level. Prior to a detailed phosphorylation analysis of a group of residues within a single protein, the impact of the protein in question is examined in terms of the entire pathway. Thus, the data-driven exploration and validation of disease mechanisms and target targets is possible without being constrained by past knowledge or assumptions of the researcher.

For inquiries regarding this matter, please contact:
SOCIUM Inc.
2-4-7 Aomi, Koto-ku, Tokyo
Rinkai Fukutoshin Center, National Institute of Advanced Industrial Science and Technology (AIST)
5th, 6th, and 7th floors, Bio-IT Fusion Research Building
https://socium.co.jp/
E-mail: contact@socium.co.jp