39635-24-0

Basic information

• Product Name: 3-hydroxy-4-methoxybenzohydrazide
• Synonyms: 3-hydroxy-4-methoxybenzohydrazide
• CAS NO: 39635-24-0
• Molecular Weight: 182.179
• Mol File: 39635-24-0.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: 3-hydroxy-4-methoxybenzohydrazide(CAS DataBase Reference)
• NIST Chemistry Reference: 3-hydroxy-4-methoxybenzohydrazide(39635-24-0)
• EPA Substance Registry System: 3-hydroxy-4-methoxybenzohydrazide(39635-24-0)

Safety Data

• Hazardous Substances Data: 39635-24-0(Hazardous Substances Data)

Upstream product

• 645-08-9 Isovanillic acid 
• 6702-50-7 3-hydroxy-4-methoxybenzoate 

Downstream Products

• 1544692-22-9 3-hydroxy-N'-(11H-indeno[1,2-b]quinoxalin-11-ylidene)-4-methoxybenzohydrazide 

Relevant articles and documents

Discovery of highly potent tubulin polymerization inhibitors: Design, synthesis, and structure-activity relationships of novel 2,7-diaryl-[1,2,4]triazolo[1,5-a]pyrimidines

By removing 5-methyl and 6-acetyl groups in our previously reported compound 3, we designed a series of novel 2,7-diaryl-[1,2,4]triazolo[1,5-a]pyrimidine derivatives as potential tubulin polymerization inhibitors. Among them, compound 5e displayed low nanomolar antiproliferative efficacy on HeLa cells which was 166-fold higher than the lead analogue 3. Interestingly, 5e displayed significant selectivity in inhibiting cancer cells over HEK-293 (normal human embryonic kidney cells). In addition, 5e dose-dependently arrested HeLa in G2/M phase through the alterations of the expression levels of p-cdc2 and cyclin B1, and caused HeLa cells apoptosis by regulation of expressions of cleaved PARP. Further evidence demonstrated that 5e effectively inhibited tubulin polymerization and was 3-fold more powerful than positive control CA-4. Moreover, molecular docking analysis indicated that 5e overlapped well with CA-4 in the colchicine-binding site. These studies demonstrated that 2,7-diaryl-[1,2,4]triazolo[1,5-a]pyrimidine skeleton might be used as the leading unit to develop novel tubulin polymerization inhibitors as potential anticancer agents.

Identification of novel urease inhibitors by high-throughput virtual and in vitro screening

Ureases are important in both agriculture and human health. Bacterial ureases are directly involved in many farm-field problems and pathological conditions. Here, we report a structure-based virtual screening of an in-house compound bank of about 6000 molecular entities by computational docking and binding free energy calculations followed by in vitro screening. Applied protocol leads to the identification of novel urease inhibitors, which can serve as starting points for structural optimization.