147682-51-7

Usage

Uses

Used in Organic Synthesis:
Benzenesulfonyl chloride, 4-hydroxy-3-nitro(9CI) is used as a building block for the synthesis of more complex organic molecules, facilitating the introduction of the sulfonyl group into various organic compounds.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, Benzenesulfonyl chloride, 4-hydroxy-3-nitro(9CI) is used as a reagent for specific chemical reactions, contributing to the development of new pharmaceuticals. Its presence of hydroxyl and nitro groups makes it a promising candidate for the creation of drugs with diverse therapeutic applications.

InChI:InChI=1/C6H4ClNO5S/c7-14(12,13)4-1-2-6(9)5(3-4)8(10)11/h1-3,9H

Upstream product

• 88-75-5 2-hydroxynitrobenzene 
• 91-23-6 2-Nitroanisole 

Downstream Products

• 30837-00-4 4-hydroxy-N-(4-methoxyphenyl)-3-nitrobenzenesulfonamide 
• 61712-36-5 3-bromo-4-hydroxy-N,N-dimethyl-5-nitrobenzenesulfonamide 
• 42247-91-6 4-hydroxy-N,N-dimethyl-3-nitrobenzenesulfonamide 
• 80-23-9 3-amino-4-hydroxy-N-methylbenzenesulfonamide 
• 96-58-2 4-hydroxy-N-methyl-3-nitrobenzenesulfonamide 
• 1097090-32-8 C₁₁H₁₄N₂O₅S 

Relevant academic research and scientific papers

C-TERMINAL SRC KINASE INHIBITORS

Provided herein are novel C-terminal Srk Kinase (CSK) inhibitors, e.g., having Formula G, I, II, or III. Also provided are methods of preparing the novel CSK inhibitors and method of using the novel CSK inhibitors for treating diseases or disorder such as cancer or for promoting immune response in a subject in need thereof. (G)

Targeting of Fumarate Hydratase from Mycobacterium tuberculosis Using Allosteric Inhibitors with a Dimeric-Binding Mode

With the growing worldwide prevalence of antibiotic-resistant strains of tuberculosis (TB), new targets are urgently required for the development of treatments with novel modes of action. Fumarate hydratase (fumarase), a vulnerable component of the citric acid cycle in Mycobacterium tuberculosis (Mtb), is a metabolic target that could satisfy this unmet demand. A key challenge in the targeting of Mtb fumarase is its similarity to the human homolog, which shares an identical active site. A potential solution to this selectivity problem was previously found in a high-throughput screening hit that binds in a nonconserved allosteric site. In this work, a structure-activity relationship study was carried out with the determination of further structural biology on the lead series, affording derivatives with sub-micromolar inhibition. Further, the screening of this series against Mtb in vitro identified compounds with potent minimum inhibitory concentrations.

A novel method for the preparation of 3-amino-4-hydroxybenzenesulfonamide percursors of 'acid alizarin violet N' derivatives

Chlorosulfonation of 2-nitroanisole gave 4-methoxy-3-nitrobenzenesulfonyl chloride (7) which was converted with N-butyl(3-phenylpropyl)amine into benzenesulfonamide (8). Hydrolysis of the ether and reduction of the nitro group of 8 followed by diazotization and coupling with 2-naphthol gave N-butyl-N-(3-phenylpropyl)-4-hydroxy-3-(2-hydroxy-1- naphthyl)azobenzenesulfonamide (1d).