Specific inhibition of oncogenic RAS using cell-permeable RAS-binding domains

Author:

Nomura Teiko Komori,Heishima Kazuki,Sugito Nobuhiko,Sugawara Ryota,Ueda Hiroshi,Yukihiro Akao,Honda RyoORCID

Funder

Hitachi Global Foundation

Yasuda Memorial Medical Foundation

Japan Society for the Promotion of Science

Publisher

Elsevier BV

Subject

Clinical Biochemistry,Drug Discovery,Pharmacology,Molecular Biology,Molecular Medicine,Biochemistry

Reference36 articles.

1. A small molecule RAS-mimetic disrupts RAS association with effector proteins to block signaling;Athuluri-Divakar;Cell,2016

2. Quantitative structure-activity analysis correlating Ras/Raf interaction in vitro to Raf activation in vivo;Block;Nat. Struct. Mol. Biol.,1996

3. Two distinct Raf domains mediate interaction with Ras;Brtva;J. Biol. Chem.,1995

4. The KRASG12C inhibitor, MRTX849, provides insight toward therapeutic susceptibility of KRAS mutant cancers in mouse models and patients;Christensen;Cancer Discov.,2019

5. Macropinocytosis of protein is an amino acid supply route in Ras-transformed cells;Commisso;Nature,2013

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