5651-01-4

Upstream product

• 5332-24-1 3-bromoquinoline 
• 59-31-4 2-quinolone 
• 529-37-3 4(1H)-quinolinone 
• 861609-06-5 N¹-(2-carboxyphenyl)-N²-phenyloxalamide 
• 144-62-7 oxalic acid 
• 118-92-3 anthranilic acid 
• 51679-86-8 2-(2-amino-2-oxoacetamido)benzoic acid 
• 344413-46-3 2-chloroformyl-4H-3,1-benzoxazin-4-one 
• 3342-77-6 N-formylanthranilic acid 
• 79-37-8 oxalyl dichloride 
• 70254-43-2 4-Hydroxy-2-quinolone 
• 7732-18-5 water 
• 861357-59-7 3-bromo-4-hydroxy-quinoline-2-carboxylic acid 
• 4169-19-1 1-acetyl-1,2,3,4-tetrahydroquinoline 

Downstream Products

• 69065-89-0 methyl N-(2-methoxycarbonylphenyl)oxalamate 
• 144-62-7 oxalic acid 
• 118-92-3 anthranilic acid 
• 612-42-0 phenylglycine-o-carboxylic acid 

Relevant academic research and scientific papers

Inhibitors of fumarylacetoacetate hydrolase domain containing protein 1 (Fahd1)

FAH domain containing protein 1 (FAHD1) acts as oxaloacetate decarboxylase in mitochondria, contributing to the regulation of the tricarboxylic acid cycle. Guided by a high-resolution X-ray structure of FAHD1 liganded by oxalate, the enzymatic mechanism of substrate processing is analyzed in detail. Taking the chemical features of the FAHD1 substrate oxaloacetate into account, the potential inhibitor structures are deduced. The synthesis of drug-like scaffolds afforded first-generation FAHD1-inhibitors with activities in the low micromolar IC50 range. The investigations disclosed structures competing with the substrate for binding to the metal cofactor, as well as scaffolds, which may have a novel binding mode to FAHD1.

Discovery and SAR of a novel selective and orally bioavailable nonpeptide classical competitive inhibitor class of protein-tyrosine phosphatase 1B

Reversible phosphorylation and dephosphorylation of key proteins on tyrosine residues are important parts of intracellular signaling triggered by hormones and other agents. Recent knock-out studies in mice have identified PTP1B as a potential target for t

Modulators of protein tyrosine phosphatases (PTPases)

The present invention provides novel compounds of Formula 1, compositions containing these compounds, methods of their use, and methods of their manufacture, where such compounds are pharmacologically useful inhibitors of Protein Tyrosine Phosphatases (PTPase's) such as PTP1B, CD45, SHP-1, SHP-2, PTPα, LAR and HePTP or the like, wherein A, R1, R2, R3, R4, R16and R17are as defined in the specification. The compounds are useful in the treatment of type I diabetes, type II diabetes, impaired glucose tolerance, insulin resistance, obesity, immune dysfunctions including autoimmunity diseases with dysfunctions of the coagulation system, allergic diseases including asthma, osteoporosis, proliferative disorders including cancer and psoriasis, diseases with decreased or increased synthesis or effects of growth hormone, diseases with decreased or increased synthesis of hormones or cytokines that regulate the release of/or response to growth hormone, diseases of the brain including Alzheimer's disease and schizophrenia, and infectious diseases.

Cyclization of N-acylanthranilic acids with Vilsmeier reagents. Chemical and structural studies

Vilsmeier reagents, generated from e.g. N,N-dimethylformamide and oxalyl chloride, reacts with N-acetylanthranilic acid to produce the 2-(2'-dimethylamino)ethenyl-4H-3,1-benzoxazin-4-one 13a. N-phenylacetylanthranilic acid similarly gave 2-(2'-dimethyl-am