10098-40-5

Usage

Uses

Used in Pharmaceutical Industry:
4-Acetamido-3-hydroxybenzoic acid is used as a reactant for the preparation of (aminophenyl)benzothiazoles, which possess cytotoxic and antitumor activities. These compounds have potential applications in the development of new drugs for the treatment of cancer, making 4-Acetamido-3-hydroxybenzoic acid a valuable building block in the pharmaceutical industry.
Used in Chemical Synthesis:
In the field of chemical synthesis, 4-Acetamido-3-hydroxybenzoic acid serves as a key intermediate for the production of various compounds with diverse applications. Its reactivity and functional groups make it a useful starting material for the synthesis of dyes, pigments, and other specialty chemicals.
Used in Research and Development:
4-Acetamido-3-hydroxybenzoic acid is also utilized in research and development for the study of its chemical properties, reactivity, and potential applications in various fields. Researchers can use 4-Acetamido-3-hydroxybenzoic acid to explore new synthetic routes, develop novel compounds, and investigate its biological activities.

Upstream product

• 619-14-7 3-hydroxy-4-nitro-benzoic acid 
• 2374-03-0 4-aminosalicylic acid 
• 75-36-5 acetyl chloride 
• 39267-53-3 methyl 4-acetamido-3-hydroxybenzoate 
• 6313-39-9 4-acetamido-3-nitro-benzoic acid methyl ester 
• 3987-92-6 methyl 4-amino-3-nitrobenzoate 
• 1588-83-6 4-amino-3-nitrobenzoic acid 
• 136663-23-5 methyl 2-methyl-1,3-benzoxazole-6-carboxylate 
• 162252-43-9 3-Acetoxy-4-(acetylamino)benzoic acid 
• 108-24-7 acetic anhydride 

Downstream Products

• 39267-53-3 methyl 4-acetamido-3-hydroxybenzoate 

Relevant academic research and scientific papers

Design and Synthesis of a Highly Selective and in Vivo-Capable Inhibitor of the Second Bromodomain of the Bromodomain and Extra Terminal Domain Family of Proteins

Pan-bromodomain and extra terminal domain (BET) inhibitors interact equipotently with the eight bromodomains of the BET family of proteins and have shown profound efficacy in a number of in vitro phenotypic assays and in vivo pre-clinical models in inflam

Identification of ortho-hydroxy anilide as a novel scaffold for lysine demethylase 5 inhibitors

Fe(II)/α-ketoglutarate-dependent lysine demethylases (KDMs) are attractive drug targets for several diseases including cancer. In this study, we designed and screened ortho-substituted anilides that are expected to function as Fe(II) chelators, and identified ortho-hydroxy anilide as a novel scaffold for KDM5A inhibitors. Treatment of human lung cancer A549 cells with a prodrug form of 4-carboxy-2-hydroxy-formanilide (9c) increased trimethylated lysine 4 on histone H3 level, suggesting KDM5 inhibition in the cells.

BENZAMIDE DERIVATIVES AS INHIBITORS OF HISTONE DEACETYLASE

The invention relates to the inhibition of histone deacetylase. The invention provides compounds which are derivatives of benzamide and suitable in methods for inhibiting histone deacetylase enzymatic activity. The invention also provides compositions and methods for treating cell proliferative diseases and conditions .

Methods of inhibiting bacterial sialidase

A method of inhibiting bacterial sialidase comprising administering to a subject an inhibiting effective amount of a compound of formula I: STR1 wherein A is CO2 H, PO2 H, or SO2 H; B is N; R1 and R2

Structure-Based Inhibitors of Influenza Virus Salidase. A Benzoic Acid Lead with Novel Interaction

Influenza virus sialidase is a surface enzyme that is essential for infection of the virus.The catalytic site is highly conserved among all known influenza variants, suggesting that this protein is a suitable target for drug intervention.The most potent known inhibitors are analogs of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en), particulary the 4-guanidino derivative (4-guanidino-Neu5Ac2en).We utilized the benzene ring of 4-(N-acetylamino)benzoic acids as a cyclic template to substitute for the dihydropyran ring of Neu5Ac2en.In this study several 3-(N-acylamino) derivatives were prepared as potential replacements for the glycerol side chain of Neu5Ac2en, and some were found to interact with the same binding subsite of sialidase.Of greater significance was the observation that the 3-guanidinobenzoic acid derivative (equivalent to the 4-guanidino grouping of 4-guanidino-Neu5Ac2en), the most potent benzoic acid inhibitor of influenza sialidase thus far identified (IC50 = 10 μM), occupied the glycerol-binding subsite on sialidase as opposed to the guanidino-binding subsite.This benzoic acid derivative thus provides a new compound that interacts in a novel manner with the catalytic site of influenza sialidase.

INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE AND METHODS OF MAKING AND USING THE SAME

An influenza virus neuraminidase inhibitor, its analogs, its pharmaceutically acceptable salts, derivatives, and mixtures thereof having the following formula: STR1 where A is CO 2 H, CO 2 H 3, NO 2, SO 3 H or PO 3 H 2, B is CH, N, O or S, R 1 and R 2 are