3-(1-(3-(biphenyl-4-ylamino)-3-oxopropyl)-1h-1-2-3-triazol-4-yl)-6-hydroxy-1-methyl-2-phenyl-1h-indole-5-carboxylic-acid and Neoplasms

3-(1-(3-(biphenyl-4-ylamino)-3-oxopropyl)-1h-1-2-3-triazol-4-yl)-6-hydroxy-1-methyl-2-phenyl-1h-indole-5-carboxylic-acid has been researched along with Neoplasms* in 2 studies

Reviews

1 review(s) available for 3-(1-(3-(biphenyl-4-ylamino)-3-oxopropyl)-1h-1-2-3-triazol-4-yl)-6-hydroxy-1-methyl-2-phenyl-1h-indole-5-carboxylic-acid and Neoplasms

ArticleYear
Strategies Targeting Protein Tyrosine Phosphatase SHP2 for Cancer Therapy.
    Journal of medicinal chemistry, 2022, 02-24, Volume: 65, Issue:4

    The protein tyrosine phosphatase SHP2 encoded by

    Topics: Animals; Antineoplastic Agents; Drug Design; Drug Discovery; Enzyme Inhibitors; Humans; Neoplasms; Protein Tyrosine Phosphatase, Non-Receptor Type 11

2022

Other Studies

1 other study(ies) available for 3-(1-(3-(biphenyl-4-ylamino)-3-oxopropyl)-1h-1-2-3-triazol-4-yl)-6-hydroxy-1-methyl-2-phenyl-1h-indole-5-carboxylic-acid and Neoplasms

ArticleYear
Salicylic acid based small molecule inhibitor for the oncogenic Src homology-2 domain containing protein tyrosine phosphatase-2 (SHP2).
    Journal of medicinal chemistry, 2010, Mar-25, Volume: 53, Issue:6

    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.

    Topics: Animals; Apoptosis; Area Under Curve; Cell Line; Cell Line, Tumor; Cells, Cultured; Crystallography, X-Ray; Enzyme Inhibitors; Female; Humans; Indoles; Inhibitory Concentration 50; Mice; Mice, Inbred C57BL; Mice, Nude; Models, Chemical; Models, Molecular; Molecular Structure; Mutation; Neoplasms; Protein Binding; Protein Structure, Tertiary; Protein Tyrosine Phosphatase, Non-Receptor Type 11; Salicylic Acid; Small Molecule Libraries; Triazoles; Xenograft Model Antitumor Assays

2010