21419-48-7Relevant articles and documents
An organometallic inhibitor for the human repair enzyme 7,8-dihydro-8-oxoguanosine triphosphatase
Streib, Manuel,Kraeling, Katja,Richter, Kristin,Xie, Xiulan,Steuber, Holger,Meggers, Eric
, p. 305 - 309 (2014)
The probe-based discovery of the first small-molecule inhibitor of the repair enzyme 8-oxo-dGTPase (MTH1) is presented, which is an unconventional cyclometalated ruthenium half-sandwich complex. The organometallic inhibitor with low-nanomolar activity displays astonishing specificity, as verified in tests with an extended panel of protein kinases and other ATP binding proteins. The binding of the organometallic inhibitor to MTH1 is investigated by protein crystallography. Not a canonical inhibitor: A ruthenium complex has been shown to be a low-nanomolar and selective inhibitor of an enzyme that hydrolyzes oxidized purine nucleoside triphosphates. This work provides a blueprint for the discovery and development of organometallic inhibitors of other purine nucleotide binding proteins which rely on ruthenium-coordinated adenine and quinazoline derivatives with tailored coordination spheres. Copyright
Microwave-assisted thermal decomposition of formamide: A tool for coupling a pyrimidine ring with an aromatic partner
Loidreau, Yvonnick,Besson, Thierry
experimental part, p. 4852 - 4857 (2011/08/06)
Rapid and efficient generation of CO and NH3 in the reaction mixture via microwave-assisted thermal decomposition of formamide may represent a significant improvement over existing methods for coupling a pyrimidine ring with an aromatic partner. This work aims at alerting readers on the probability to observe interesting phenomena and reactions when this very powerful heating mode is associated with thermally unstable reagents.