Li, Haishan Hah, Jung-Mi Lawrence, David S. 2024-01-20T23:00:28Z 2024-01-20T23:00:28Z 2021-08-31 2008-08-13 0002-7863 https://pubs.kist.re.kr/handle/201004/133232 Light-activatable ("caged") proteins have been used to correlate, with exquisite temporal and spatial control, intracellular biochemical action with global cellular behavior. However, the chemical or genetic construction of caged proteins is nontrivial, with subsequent laborious introduction into living cells, potentially problematic competition with natural endogenous counterparts, and challenging intracellular incorporation at levels equivalent to the natural enzymes. We describe the design, synthesis, and characterization of small molecular equivalents of a caged Src kinase. These compounds are easy to prepare and function by inhibiting the action of the natural unmodified enzyme. English AMER CHEMICAL SOC CATALYTIC SUBUNIT TYROSINE KINASES ACQUISITION Light-mediated liberation of enzymatic activity: "Small Molecule" caged protein equivalents Article 10.1021/ja803395d 1 JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, v.130, no.32, pp.10474 - + JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 130 32 10474 + scie scopus 000258293800013 2-s2.0-49449113694 Chemistry, Multidisciplinary Chemistry Article CATALYTIC SUBUNIT TYROSINE KINASES ACQUISITION Caging Kinase bivalent inhibitor