10169-50-3Relevant articles and documents
Rearrangements during nitrosodecarboxylation of isomeric dibromohydroxybenzoic acids
Shishkin,Fadin
, p. 688 - 692 (2008)
The reaction of 3,5-dibromo-4-hydroxybenzoic acid, its sodium salt, and also sodium 3,5-dibromo-2-hydroxybenzoate with NaNO2 in a glacial acetic acid at room temperature led to the formation of a mixture of dibromonitrophenol resulting from nitrosodecarboxylation accompanied by a rearrangement processes and followed by oxidation of the arising nitrosophenols.
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.
, p. 1020 - 1023 (2019)
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.
3-process for the preparation of amino-salicylic acid
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Paragraph 0029-0031, (2016/10/08)
The invention relates to a novel preparation method of 3-aminosalicylic acid. The novel preparation method is characterized in that a salicylic acid compound I as an initial raw material having a general formula shown in the description and a nitration agent undergo a reaction to produce a 3-nitrosalicylic acid compound II having a general formula shown in the description, and the 3-nitrosalicylic acid compound II undergoes nitryl catalytic hydrogenation reduction and dehalogenation hydrogenolysis reactions in the presence of an effective dose of a catalyst and hydrogen donors so that 3-aminosalicylic acid is produced.
Discovery of potent, selective chymase inhibitors via fragment linking strategies
Taylor, Steven J.,Padyana, Anil K.,Abeywardane, Asitha,Liang, Shuang,Hao, Ming-Hong,De Lombaert, Stéphane,Proudfoot, John,Farmer, Bennett S.,Li, Xiang,Collins, Brandon,Martin, Leslie,Albaugh, Daniel R.,Hill-Drzewi, Melissa,Pullen, Steven S.,Takahashi, Hidenori
, p. 4465 - 4481 (2013/07/19)
Chymase plays an important and diverse role in the homeostasis of a number of cardiovascular processes. Herein, we describe the identification of potent, selective chymase inhibitors, developed using fragment-based, structure-guided linking and optimizati