134796-49-9Relevant academic research and scientific papers
TARGETED COVALENT PROBES AND INHIBITORS OF PROTEINS CONTAINING REDOX-SENSITIVE CYSTEINES
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Paragraph 00143-00144, (2014/06/24)
Covalent, irreversible small-molecule inhibitors that modify the sulfenyl form (i.e., sulfenic acid, RSOH and sulfenamide, RSNR'2) of therapeutically important proteins (particularly kinases and phosphatases) are disclosed, where the compositions include a compound having a substituted aryl or heterocyclic core structure that promotes binding interactions with a specific protein, and a nucleophilic reaction center (carbon, nitrogen, sulfur, or phosphorous) that is capable of forming a covalent bond with a sulfenic acid- or sulfenamide-modified cysteine residue in the protein. Methods for synthesizing these compounds are also disclosed, as well as methods of using them for determining the bioactivity of a chemical composition comprising an active compound toward a specific protein and for determining the potency of an inhibitor against a specific protein.
Synthesis of fused oxabicyclic systems by metal-catalyzed intramolecular addition of 1,3-cycloalkyldiones to alkynes
Gulias, Moises,Rodriguez, J. Ramon,Castedo, Luis,Mascarenas, Jose L.
, p. 1975 - 1977 (2007/10/03)
(Matrix presented) Readily available 4-propargyl-1,3-cyclohexanediones and cyclopentanediones can be chemo- and regioselectively cycloisomerized to synthetically appealing fused oxabicyclic systems by simply stirring at room temperature with catalytic amounts of an appropriate metal complex.
