1143579-91-2

Upstream product

• 1143579-89-8 methyl 4-(dimethylamino)-2-hydroxy-5-iodobenzoate 
• 536-74-3 phenylacetylene 

Downstream Products

• 1143579-93-4 methyl 6-hydroxy-3-iodo-1-methyl-2-phenyl-1 H-indole-5-carboxylate 
• 1404436-71-0 6-hydroxy-3-iodo-1-methyl-2-phenyl-1H-indole-5-carboxylic acid 

Relevant academic research and scientific papers

TYROSINE PHOSPHATASE INHIBITORS AND USES THEREOF TO MODULATE THE ACTIVITY OF LYP

A variety of benzofurans and indole derivatives some with an acetyl linker are disclosed herein. These compounds are not highly charged at physiological pH and have good bioavailability characteristics. These compounds exhibit selective or at least preferential affinity for the active sites of various sub-sets of protein tyrosine phosphatases. The lymphoid- specific tyrosine phosphatase (Lyp) has received enormous attention because of the finding that a single- nucleotide polymorphism (SNP) in the gene (PTPN22) encoding Lyp is associated with several autoimmune diseases, including type I diabetes. Many of these compounds and pharmaceutically acceptable salts thereof are novel therapeutic compounds useful for the treatment of various diseases including a number of autoimmune diseases.

Salicylic acid based small molecule inhibitor for the oncogenic src homology-2 domain containing protein tyrosine phosphatase-2 (SHP2)

The Src homology-2 domain containing protein tyrosine phosphatase-2 (SHP2) plays a pivotal role in growth factor and cytokine signaling. Gain-of-function SHP2 mutations are associated with Noonan syndrome, various kinds of leukemias, and solid tumors. Thus, there is considerable interest in SHP2 as a potential target for anticancer and antileukemia therapy. We report a salicylic acid based combinatorial library approach aimed at binding both active site and unique nearby subpockets for enhanced affinity and selectivity. Screening of the library led to the identification of a SHP2 inhibitor II-B08 (compound 9) with highly efficacious cellular activity. Compound 9 blocks growth factor stimulated ERK1/2 activation and hematopoietic progenitor proliferation, providing supporting evidence that chemical inhibition of SHP2 may be therapeutically useful for anticancer and antileukemia treatment. X-ray crystallographic analysis of the structure of SHP2 in complex with 9 reveals molecular determinants that can be exploited for the acquisition of more potent and selective SHP2 inhibitors.