1456809-37-2Relevant academic research and scientific papers
Systemic optimization and structural evaluation of quinoline derivatives as transthyretin amyloidogenesis inhibitors
Kim, Boyoung,Park, Hwanggue,Lee, Seul Ki,Park, Sung Jean,Koo, Tae-Sung,Kang, Nam Sook,Hong, Ki Bum,Choi, Sungwook
, p. 777 - 787 (2016/08/23)
Wild type transthyretin (TTR) and mutant TTR misfold and misassemble into a variety of extracellular insoluble amyloid fibril and/or amorphous aggregate, which are associated with a variety of human amyloid diseases. To develop potent TTR amyloidogenesis
Bifunctional coumarin derivatives that inhibit transthyretin amyloidogenesis and serve as fluorescent transthyretin folding sensors
Myung, Nojoon,Connelly, Stephen,Kim, Boyoung,Park, Sung Jean,Wilson, Ian A.,Kelly, Jeffery W.,Choi, Sungwook
supporting information, p. 9188 - 9190 (2013/09/24)
We describe coumarin derivatives that are non-fluorescent in aqueous buffers and that very selectively bind to transthyretin (TTR) in complex biological environments potently inhibiting TTR amyloidogenesis while also exhibiting sensitive off-on fluorescen
