5335-97-7

Usage

Uses

Used in Pharmaceutical Industry:
4-[(8-hydroxyquinolin-7-yl)(phenyl)methyl]aminobenzoic acid is used as a therapeutic agent for its potential anti-inflammatory and antioxidant properties, making it a candidate for the treatment of various diseases.
Used in Oncology:
In the field of oncology, 4-[(8-hydroxyquinolin-7-yl)(phenyl)methyl]aminobenzoic acid is used as a potential anti-cancer agent, given its capacity to target and treat cancer cells while exhibiting less toxicity to normal cells.
Used in Neurodegenerative Disorder Treatment:
4-[(8-hydroxyquinolin-7-yl)(phenyl)methyl]aminobenzoic acid is utilized as a neuroprotective agent, leveraging its potential to mitigate the effects of neurodegenerative disorders by combating oxidative stress and inflammation.
Used in Inflammatory Conditions Management:
For the management of inflammatory conditions, 4-[(8-hydroxyquinolin-7-yl)(phenyl)methyl]aminobenzoic acid is applied as an anti-inflammatory agent, helping to reduce inflammation and associated symptoms.
These applications highlight the compound's versatility and potential impact on various areas of medicine, warranting further research to fully understand and harness its therapeutic capabilities.

Upstream product

• 148-24-3 8-quinolinol 
• 100-52-7 benzaldehyde 
• 150-13-0 4-amino-benzoic acid 

Downstream Products

• 108987-30-0 {Ni(C₂₃H₁₇N₂O₃)2} 

Relevant academic research and scientific papers

8-Hydroxyquinoline-based inhibitors of the Rce1 protease disrupt Ras membrane localization in human cells

Ras converting enzyme 1 (Rce1) is an endoprotease that catalyzes processing of the C-terminus of Ras protein by removing -aaX from the CaaX motif. The activity of Rce1 is crucial for proper localization of Ras to the plasma membrane where it functions. Ras is responsible for transmitting signals related to cell proliferation, cell cycle progression, and apoptosis. The disregulation of these pathways due to constitutively active oncogenic Ras can ultimately lead to cancer. Ras, its effectors and regulators, and the enzymes that are involved in its maturation process are all targets for anti-cancer therapeutics. Key enzymes required for Ras maturation and localization are the farnesyltransferase (FTase), Rce1, and isoprenylcysteine carboxyl methyltransferase (ICMT). Among these proteins, the physiological role of Rce1 in regulating Ras and other CaaX proteins has not been fully explored. Small-molecule inhibitors of Rce1 could be useful as chemical biology tools to understand further the downstream impact of Rce1 on Ras function and serve as potential leads for cancer therapeutics. Structure-activity relationship (SAR) analysis of a previously reported Rce1 inhibitor, NSC1011, has been performed to generate a new library of Rce1 inhibitors. The new inhibitors caused a reduction in Rce1 in vitro activity, exhibited low cell toxicity, and induced mislocalization of EGFP-Ras from the plasma membrane in human colon carcinoma cells giving rise to a phenotype similar to that observed with siRNA knockdowns of Rce1 expression. Several of the new inhibitors were more effective at mislocalizing K-Ras compared to a potent farnesyltransferase inhibitor (FTI), which is significant because of the preponderance of K-Ras mutations in cancer.