38399-46-1Relevant academic research and scientific papers
Small-molecules that covalently react with a human prolyl hydroxylase-towards activity modulation and substrate capture
Bush, Jacob T.,Le?niak, Robert K.,Yeh, Tzu-Lan,Belle, Roman,Kramer, Holger,Tumber, Anthony,Chowdhury, Rasheduzzaman,Flashman, Emily,Mecinovi?, Jasmin,Schofield, Christopher J.
supporting information, p. 1020 - 1023 (2019/01/28)
We describe covalently binding modulators of the activity of human prolyl hydroxylase domain 2 (PHD2) and studies towards a strategy for photocapture of PHD2 substrates. Reversible active site binding of electrophile bearing compounds enables susbsequent covalent reaction with a lysine residue (K408) in the flexible C-terminal region of PHD2 to give a modified protein that retains catalytic activity.
Azomethine pigments
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, (2008/06/13)
Azomethine pigments of the formula SPC1 And metal complexes thereof, wherein A denotes an isocyclic or heterocyclic aromatic radical, R denotes a H atom, an alkyl group containing 1-6 C atoms, or an aryl radical, X2 and X4 denote H atoms or halogen atoms, X1 and X3 denote H atoms or halogen atoms, alkoxy or alkylmercapto groups containing 1-6 C atoms, cycloalkoxy groups containing 5-6 C atoms, or aralkoxy, aryloxy or arylmercapto groups, it being possible for one of the substituents X1 -X4 also to be a nitro group which are useful for pigmenting of high molecular material.
