Lim, Yun Kim, Ji Yul Jung, Youn Hee Lee, Jae Hoon Baek, Min Seok Jung, Je Hyeong Kim, Ho-Youn Lee, Wookbin Park, Keunwan Seo, Moon-Hyeong 2024-01-12T06:34:34Z 2024-01-12T06:34:34Z 2023-05-24 2023-09 0925-4005 https://pubs.kist.re.kr/handle/201004/79851 Studies on glutamine (Gln) metabolism have highlighted the vital role of Gln in cellular functions and its potential as a biomarker for disease detection. Despite the increasing interest in Gln metabolism, in-depth evaluations are challenging owing to the limitations of conventional Gln-measuring methods. Thus, we developed a ligand-induced dimerization-based sensor for Gln, termed Q-SHINE, by splitting a glutamine-binding protein into two separate domains. Q-SHINE enables the highly accurate and convenient measurement of Gln concentrations in bio-fluid samples, with an optimal detection range for physiological Gln levels. Genetically encoded Q-SHINE sensors could also visualize intracellular Gln levels and quantify cytoplasmic and mitochondrial Gln changes in living cells, enabling the detection of various cell responses to extracellular Gln supplementation. English Elsevier BV Q-SHINE: A versatile sensor for glutamine measurement via ligand-induced dimerization Article 10.1016/j.snb.2023.133951 1 Sensors and Actuators, B: Chemical, v.390 Sensors and Actuators, B: Chemical 390 Y scie scopus 001113615100001 Chemistry, Analytical Electrochemistry Instruments & Instrumentation Chemistry Electrochemistry Instruments & Instrumentation Article TRANSPORTER METABOLISM HISTIDINE GROWTH SLC1A5 SERUM AGE AMINO-ACID LEVELS PROTEIN Glutamine Biosensor Periplasmic binding protein Chemically induced dimerization Glutamine-binding protein